ID A0A1Z4NKY1_9CYAN Unreviewed; 483 AA.
AC A0A1Z4NKY1;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Nickel-dependent hydrogenase large subunit {ECO:0000313|EMBL:BAZ06360.1};
GN ORFNames=NIES3974_30210 {ECO:0000313|EMBL:BAZ06360.1};
OS Calothrix sp. NIES-3974.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=2005462 {ECO:0000313|EMBL:BAZ06360.1, ECO:0000313|Proteomes:UP000218621};
RN [1] {ECO:0000313|EMBL:BAZ06360.1, ECO:0000313|Proteomes:UP000218621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-3974 {ECO:0000313|EMBL:BAZ06360.1,
RC ECO:0000313|Proteomes:UP000218621};
RA Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT "Genome sequencing of cyanobaciteial culture collection at National
RT Institute for Environmental Studies (NIES).";
RL Submitted (JUN-2017) 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|PIRSR:PIRSR601501-1};
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DR EMBL; AP018254; BAZ06360.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z4NKY1; -.
DR OrthoDB; 9761717at2; -.
DR Proteomes; UP000218621; Chromosome.
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; PTHR43600; COENZYME F420 HYDROGENASE, SUBUNIT ALPHA; 1.
DR PANTHER; PTHR43600:SF2; CYTOSOLIC NIFE-HYDROGENASE, ALPHA SUBUNIT; 1.
DR Pfam; PF00374; NiFeSe_Hases; 2.
DR SUPFAM; SSF56762; HydB/Nqo4-like; 1.
DR PROSITE; PS00508; NI_HGENASE_L_2; 1.
PE 4: Predicted;
KW Iron {ECO:0000256|PIRSR:PIRSR601501-1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR601501-1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR601501-1};
KW Nickel {ECO:0000256|PIRSR:PIRSR601501-1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Quinone {ECO:0000256|ARBA:ARBA00022719};
KW Reference proteome {ECO:0000313|Proteomes:UP000218621}.
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 406
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 452
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 455
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 458
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
SQ SEQUENCE 483 AA; 53758 MW; 31E57411553E5D17 CRC64;
MSKKIIIDPV TRIEGHAKIS IYLDDSGQVS NARFHVTEFR GFEKFCQGRP LWEMPGITAR
ICGICPVSHL LASAKAGDRI LAVNIPKAAE KLRRLMNLAQ IIQSHALSFF HLSAPDLLLG
MDSEPSQRNL FGLIAAEPEL ARGGIRLRQF GQEIIELLGG RKIHPSWAVP GGVREALSPE
GRTQIQNRIS EARNIILDAL ARFKQLLNKY QQEIQTFGNF PSLFMGLVTP TGLWEHYDGY
IRFVDSGGNI IADKLDPNCY REFIAEAVEP DSYLKSPYYR PLGYPDSRAS CLLDSGMYRV
GSLARLNICT HIGTDLADRE LREFRDIGQG VVTSSFFYHY ARLIEILAAI ERIEILLDDP
DILSNRLRAD AGINQLEGIG VSEAPRGTLF HHYQVDENGL IQQVNLIIAT GQNNLAMNRT
IAQIARYFIH GSDIPEGMLN RVEAGIRAFD PCLSCSTHAV GQMPLHVELV GADGSVLNEA
WRN
//
