ID V6F1T6_MAGGM Unreviewed; 568 AA.
AC V6F1T6;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Uptake hydrogenase large subunit {ECO:0000313|EMBL:CDK99409.1};
DE EC=1.12.99.6 {ECO:0000313|EMBL:CDK99409.1};
GN Name=hupL {ECO:0000313|EMBL:CDK99409.1};
GN OrderedLocusNames=MGMSRv2__2194 {ECO:0000313|EMBL:CDK99409.1};
OS Magnetospirillum gryphiswaldense (strain DSM 6361 / JCM 21280 / NBRC 15271
OS / MSR-1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=431944 {ECO:0000313|EMBL:CDK99409.1, ECO:0000313|Proteomes:UP000018922};
RN [1] {ECO:0000313|EMBL:CDK99409.1, ECO:0000313|Proteomes:UP000018922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1
RC {ECO:0000313|Proteomes:UP000018922};
RX PubMed=24625872; DOI=10.1128/genomeA.00171-14;
RA Wang X., Wang Q., Zhang W., Wang Y., Li L., Wen T., Zhang T., Zhang Y.,
RA Xu J., Hu J., Li S., Liu L., Liu J., Jiang W., Tian J., Li Y., Schuler D.,
RA Wang L., Li J.;
RT "Complete genome sequence of Magnetospirillum gryphiswaldense MSR-1.";
RL Genome Announc. 2:e00171-e00114(2014).
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}.
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; HG794546; CDK99409.1; -; Genomic_DNA.
DR AlphaFoldDB; V6F1T6; -.
DR STRING; 1430440.MGMSRv2__2194; -.
DR KEGG; mgy:MGMSRv2__2194; -.
DR eggNOG; COG0374; Bacteria.
DR HOGENOM; CLU_030087_0_0_5; -.
DR Proteomes; UP000018922; Chromosome I.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 PANTHER; PTHR42958; HYDROGENASE-2 LARGE CHAIN; 1.
DR PANTHER; PTHR42958:SF1; HYDROGENASE-2 LARGE CHAIN; 1.
DR Pfam; PF00374; NiFeSe_Hases; 1.
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:UP000018922}.
FT BINDING 42
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 61
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 64
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 64
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 547
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 550
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 553
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
SQ SEQUENCE 568 AA; 62286 MW; 2833703D1BF058EA CRC64;
MSKRITIDPI TRIEGHLRID VEVDNGKVTK AWSSGQMWRG VELILLGRDP RDAWAITQRI
CGVCTTVHAI TSVRAVENAL NLEVPVNAQF IRNMIASAHA LHDHIVHFYH LSALDFVDVV
SALKADPEAT SKLAESLSDW PMNSRHVMAQ TKEKLATFVG SGQLGPFANG YWGHPAMKLT
PEVNLLAVAH YLQALEAQRH ASKIVTILGS KSPHIQNLAV GGVANPIATD SQSVLTVERL
LAVKEHIDAL SEFTRKVYLP DVAAIGAFYA DWTKYGKGIT NYISSPEFPT DSKGTQFMVP
GGHIPDADLA QYKPFTAFGD QYLRDGVEES VKHAWYTYSK PGALHPYKGE TTPHYTDFQD
DGKYSWLKAP TFYGKRAQVG PLANVLCGLA AGHQPTATYA TQMLNTVSTL LGSKVGPEIL
HSTIGRHAAR AIRSGVMAEV LAQNWSMLIE NIGKGDHTTF NKPVFPKGEV MGFGMHEAPR
GLLSHWTVIK DGKIANYQCV VPSTWNAGPR DENDAIGPYE ASLMDNPIAD PEQPLEVLRT
VHSFDPCLAC AVHVHDDEKR EIVQVKAL
//
