ID G6FV44_9CYAN Unreviewed; 531 AA.
AC G6FV44;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Cytochrome-c3 hydrogenase {ECO:0000313|EMBL:EHC12099.1};
DE EC=1.12.2.1 {ECO:0000313|EMBL:EHC12099.1};
GN ORFNames=FJSC11DRAFT_2741 {ECO:0000313|EMBL:EHC12099.1};
OS Fischerella thermalis JSC-11.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Hapalosiphonaceae;
OC Fischerella.
OX NCBI_TaxID=741277 {ECO:0000313|EMBL:EHC12099.1, ECO:0000313|Proteomes:UP000004344};
RN [1] {ECO:0000313|EMBL:EHC12099.1, ECO:0000313|Proteomes:UP000004344}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JSC-11 {ECO:0000313|EMBL:EHC12099.1,
RC ECO:0000313|Proteomes:UP000004344};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Sarkisova S., Bryant D.A., Brown I.,
RA Woyke T.J.;
RT "The draft genome of Fischerella sp. JSC-11.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit
CC family. {ECO:0000256|ARBA:ARBA00009292}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHC12099.1}.
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DR EMBL; AGIZ01000008; EHC12099.1; -; Genomic_DNA.
DR RefSeq; WP_009457453.1; NZ_AGIZ01000008.1.
DR AlphaFoldDB; G6FV44; -.
DR GeneID; 60766803; -.
DR PATRIC; fig|741277.3.peg.2313; -.
DR Proteomes; UP000004344; Unassembled WGS sequence.
DR GO; GO:0047806; F:cytochrome-c3 hydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro.
DR GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
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 PANTHER; PTHR42958:SF4; HYDROGENASE EXPRESSION_FORMATION PROTEIN HUPK; 1.
DR PANTHER; PTHR42958; HYDROGENASE-2 LARGE CHAIN; 1.
DR Pfam; PF00374; NiFeSe_Hases; 2.
DR SUPFAM; SSF56762; HydB/Nqo4-like; 1.
DR PROSITE; PS00507; NI_HGENASE_L_1; 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:0000313|EMBL:EHC12099.1}; Quinone {ECO:0000256|ARBA:ARBA00022719};
KW Reference proteome {ECO:0000313|Proteomes:UP000004344}.
FT BINDING 43
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 62
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 65
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 65
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 461
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 509
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 512
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 515
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
SQ SEQUENCE 531 AA; 60208 MW; 778917D40EF558D4 CRC64;
MGTQTLDISP VGRVEGDLDV RVEIEDGYVV NAWTHAELFR GFEVILRGKD PQAGLIVTPR
ICGICGGSHL TCASWALDTA WETEVPRNAI LARNLGQIVE TIQSIPRYFY GLFAIDLTNK
KYQNSRYYNE AVRRFAAFTG KHYEIGVTIS AKPVEIYALL GGQWPHSSYM VPGGVMSAPT
LTDITRAWSI LEYFRTNWLE PVWLGCSLER YEEIQTYDDF MAWLHENRNH RQSDLGFYWR
MGLDIGLDKF GGGVGKYVTW GYLPHEDKYQ KPTIENRNAA MIMKSGVYDS YSDTHTLMDH
TFTRENTTHA WYDEGTADVH PFDRTTNPTA KNHKDFNGAY SWSSAVRHIE YGRLEAGPLA
RQLVAGGTHG ESWQHYDGFI LDVFKRMGGP SVHVRQLARV HEIVKLYRQA ERCLREFKLN
EPWYIKPKQK DGRGWGATEA ARGSLCHWVE LEDGKIKNYQ VIAPTTWNVG PRDAEQKRGP
IEEALVGIPV ADPADPIEVG HVARSFDSCL VCTVHAHDAK TGEELARFRT A
//
