ID C0QLX4_DESAH Unreviewed; 504 AA.
AC C0QLX4;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=HysA {ECO:0000313|EMBL:ACN14280.1};
DE EC=1.12.99.6 {ECO:0000313|EMBL:ACN14280.1};
GN Name=hysA {ECO:0000313|EMBL:ACN14280.1};
GN OrderedLocusNames=HRM2_11680 {ECO:0000313|EMBL:ACN14280.1};
OS Desulforapulum autotrophicum (strain ATCC 43914 / DSM 3382 / VKM B-1955 /
OS HRM2) (Desulfobacterium autotrophicum).
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulforapulum.
OX NCBI_TaxID=177437 {ECO:0000313|EMBL:ACN14280.1, ECO:0000313|Proteomes:UP000000442};
RN [1] {ECO:0000313|EMBL:ACN14280.1, ECO:0000313|Proteomes:UP000000442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43914 / DSM 3382 / HRM2
RC {ECO:0000313|Proteomes:UP000000442};
RX PubMed=19187283; DOI=10.1111/j.1462-2920.2008.01825.x;
RA Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J., Andres S.,
RA Henne A., Fricke W.F., Martinez-Arias R., Bartels D., Goesmann A.,
RA Krause L., Puehler A., Klenk H.P., Richter M., Schuler M., Gloeckner F.O.,
RA Meyerdierks A., Gottschalk G., Amann R.;
RT "Genome sequence of Desulfobacterium autotrophicum HRM2, a marine sulfate
RT reducer oxidizing organic carbon completely to carbon dioxide.";
RL Environ. Microbiol. 11:1038-1055(2009).
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|PIRSR:PIRSR601501-1};
CC -!- COFACTOR:
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000256|ARBA:ARBA00001967,
CC ECO:0000256|PIRSR:PIRSR601501-1};
CC -!- SUBUNIT: Heterodimer of a large and a small subunit.
CC {ECO:0000256|ARBA:ARBA00011771}.
CC -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit
CC family. {ECO:0000256|ARBA:ARBA00009292, ECO:0000256|RuleBase:RU003896}.
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DR EMBL; CP001087; ACN14280.1; -; Genomic_DNA.
DR STRING; 177437.HRM2_11680; -.
DR KEGG; dat:HRM2_11680; -.
DR eggNOG; COG0374; Bacteria.
DR HOGENOM; CLU_030087_0_0_7; -.
DR OrthoDB; 9761717at2; -.
DR Proteomes; UP000000442; Chromosome.
DR GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro.
DR GO; GO:0033748; F:hydrogenase (acceptor) activity; IEA:UniProtKB-EC.
DR GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR Gene3D; 1.10.645.10; Cytochrome-c3 Hydrogenase, chain B; 1.
DR InterPro; IPR001501; Ni-dep_hyd_lsu.
DR InterPro; IPR018194; Ni-dep_hyd_lsu_Ni_BS.
DR InterPro; IPR029014; NiFe-Hase_large.
DR NCBIfam; NF033181; NiFeSe_hydrog; 1.
DR PANTHER; PTHR42958; HYDROGENASE-2 LARGE CHAIN; 1.
DR PANTHER; PTHR42958:SF2; UPTAKE HYDROGENASE LARGE SUBUNIT; 1.
DR Pfam; PF00374; NiFeSe_Hases; 2.
DR SUPFAM; SSF56762; HydB/Nqo4-like; 1.
DR PROSITE; PS00507; NI_HGENASE_L_1; 1.
DR PROSITE; PS00508; NI_HGENASE_L_2; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|PIRSR:PIRSR601501-1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR601501-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR601501-1};
KW Nickel {ECO:0000256|ARBA:ARBA00022596, ECO:0000256|PIRSR:PIRSR601501-1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003896};
KW Reference proteome {ECO:0000313|Proteomes:UP000000442};
KW Selenium {ECO:0000313|EMBL:ACN14280.1};
KW Selenocysteine {ECO:0000313|EMBL:ACN14280.1}.
FT BINDING 57
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 76
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 79
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 79
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 434
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 485
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 488
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT NON_STD 482
FT /note="Selenocysteine"
FT /evidence="ECO:0000313|EMBL:ACN14280.1"
SQ SEQUENCE 504 AA; 55164 MW; FEA0009832C56EAD CRC64;
MAGCKPEAVP VGAAGKKIKV AIDPVTRIEG HLKVEVEVKG GKVVDARCFG GMFRGFENIL
TGRDPRDATQ IVQRICGVCP TAHATASSLA LDDAFGVKLT NNGRVARNLI LGANFLQSHI
LHFYHLAALD YVNGPEVAPF IPRYKNNDVR LDKATNQVGV DQYLEALEIR KICHEMVALL
GGKMPHVQGI VVGGTTEIPT REKLDAYKER FKTVRKFIEE RYLPLIYLLA GPYGDLLKTG
TGYKNCIAFG VFPLDDAGNT LLKSGVFTDG KYTDFNSDNI KEYVKHSFFA DNTTGLHPSK
GKTVPDPEKA TGYSFIKSPR YNGKPHEVGP LARMWITNPE LSATGQKALG VKRMRDIGDA
AFSILGRHIA RAEETLLVAM QMERWLEEAK PGLETFVAAP IPENAEGIGL TEAPRGALLH
YIDIKNSVIS NYQITSATIW NANPRDDMEQ RGPIEQALIG IPVPDIDSPV NVGRLIRSFD
PULGCAVHVL HAETGKTNVV EIPL
//
