KEGG ENZYME: 1.12.98.4

ENZYME: 1.12.98.4

Entry

EC 1.12.98.4                Enzyme

Name

sulfhydrogenase;
sulfur reductase

Class

Oxidoreductases;
Acting on hydrogen as donor;
With other, known, physiological acceptors

Sysname

H2:polysulfide oxidoreductase

Reaction(IUBMB)

H2 + (sulfide)n = hydrogen sulfide + (sulfide)n-1 [RN:R10390]

Reaction(KEGG)

R10390

Substrate

H2 [CPD:C00282];
(sulfide)n [CPD:C19692]

Product

hydrogen sulfide [CPD:C00283];
(sulfide)n-1

Comment

An iron-sulfur protein. The enzyme from the hyperthermophilic archaeon Pyrococcus furiosus is part of two heterotetrameric complexes where the beta and gamma subunits function as sulfur reductase and the alpha and delta subunits function as hydrogenases (EC 1.12.1.3, hydrogen dehydrogenase [NADP+] and EC 1.12.1.4, hydrogen dehydrogenase [NAD(P)+], respectively). Sulfur can also be used as substrate, but since it is insoluble in aqueous solution and polysulfide is generated abiotically by the reaction of hydrogen sulfide and sulfur, polysulfide is believed to be the true substrate [2].

History

EC 1.12.98.4 created 1992 as EC 1.97.1.3, transferred 2013 to EC 1.12.98.4

Pathway

ec00920

Sulfur metabolism

ec01120

Microbial metabolism in diverse environments

Orthology

K17995

sulfhydrogenase subunit gamma (sulfur reductase)

K17996

sulfhydrogenase subunit beta (sulfur reductase)

Genes

TOB:	V4D31_02075

TAUT:

V4D30_05980

TVX:	QBE54_05510

ATHO:

M15_09820

PFU:	PF0891 PF0892 PF1329 PF1330

PFI:	PFC_03665 PFC_03670 PFC_05860 PFC_05865

PHO:	PH1290(PH1290) PH1291(PH1291)

PAB:	PAB0638(hydB-2) PAB0639(hydG-2) PAB1784 PAB1785

PYN:	PNA2_1554 PNA2_1555 PNA2_1667 PNA2_1668

PYA:	PYCH_00020 PYCH_00030 PYCH_08390 PYCH_08400

PYS:	Py04_0890 Py04_0891 Py04_1131 Py04_1132

PYC:	TQ32_02775 TQ32_02780 TQ32_03125 TQ32_03130

TKO:	TK2071 TK2072

TON:	TON_0054 TON_0055 TON_0536 TON_0537

TSI:	TSIB_0282 TSIB_0283 TSIB_1520 TSIB_1521

TBA:	TERMP_00067 TERMP_00068 TERMP_00538 TERMP_00539

THE:	GQS_02460 GQS_02465 GQS_04975 GQS_04980

THA:	TAM4_114 TAM4_307 TAM4_579 TAM4_858

THM:	CL1_0141 CL1_0142 CL1_0641 CL1_0642

TLT:	OCC_03052 OCC_03057 OCC_12226 OCC_12231

THS:	TES1_0164 TES1_0165

TNU:	BD01_0439 BD01_0440 BD01_2065 BD01_2066

TEU:	TEU_09735 TEU_09740

TGY:	X802_03235 X802_03240 X802_07570 X802_07575

THV:	ADU37_CDS02150 ADU37_CDS02160 ADU37_CDS16300 ADU37_CDS16310

TCH:	CHITON_0947 CHITON_0948 CHITON_1017 CHITON_1018

TPEP:

A0127_05285 A0127_05290 A0127_07145 A0127_07150

TPIE:

A7C91_06195 A7C91_06200 A7C91_08735 A7C91_08740

TGG:	A3K92_08490 A3K92_08495

TCE:	A3L02_00955 A3L02_00960 A3L02_02375 A3L02_02380

TBS:	A3L01_00930 A3L01_00935 A3L01_03425 A3L01_03430

THH:	CDI07_00930 CDI07_00935 CDI07_03365 CDI07_03370

TSL:	A3L11_04685 A3L11_04690 A3L11_07385 A3L11_07390

TTD:	A3L14_02385 A3L14_02390 A3L14_05110 A3L14_05115

TPRF:

A3L09_05675 A3L09_05680 A3L09_05730 A3L09_05735

TRL:	A3L10_03140 A3L10_03145 A3L10_05625 A3L10_05630

TPAF:

A3L08_06490 A3L08_06495

THY:	A3L12_05470 A3L12_05475

TIC:	FH039_02785 FH039_02790 FH039_05980 FH039_05985

TCQ:	TIRI35C_0408(shyC) TIRI35C_0409(shyB) TIRI35C_0920(hydG) TIRI35C_0921(hydB)

THEM:

FPV09_03365 FPV09_03370 FPV09_06565 FPV09_06570

THEI:

K1720_00345 K1720_00350 K1720_04535 K1720_04540

TAGG:

NF865_01285(hydG) NF865_01290(hydB)

PPAC:

PAP_01500 PAP_01505 PAP_03240 PAP_03245

KCR:	Kcr_0323 Kcr_0324

BARB:

AOA66_1501(shyB) AOA66_1502(shyC_1)

» show all

Reference

Authors

Zophel A, Kennedy MC, Beinert H, Kroneck PMH.

Title

Investigations on microbial sulfur respiration. 1. Activation and reduction of elemental sulfur in several strains of Eubacteria.

Journal

Arch Microbiol 150:72-77 (1988)

Reference

2 [PMID:8389482]

Authors

Ma K, Schicho RN, Kelly RM, Adams MW

Title

Hydrogenase of the hyperthermophile Pyrococcus furiosus is an elemental sulfur reductase or sulfhydrogenase: evidence for a sulfur-reducing hydrogenase ancestor.

Journal

Proc Natl Acad Sci U S A 90:5341-4 (1993)
DOI:10.1073/pnas.90.11.5341

Sequence

[pfu:PF0891 PF0892]

Reference

Authors

Ma K, Zhou ZH, Adams MW.

Title

Hydrogen production from pyruvate by enzymes purified from the hyperthermophilic archaeon, Pyrococcus furiosus: A key role for NADPH.

Journal

FEMS Microbiol Lett 122:245-250 (1994)

Reference