ID A0A1D8T4X9_9NOCA Unreviewed; 430 AA.
AC A0A1D8T4X9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Dehydrogenase {ECO:0000313|EMBL:AOW92644.1};
GN ORFNames=BFN03_07920 {ECO:0000313|EMBL:AOW92644.1};
OS Rhodococcus sp. WMMA185.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=679318 {ECO:0000313|EMBL:AOW92644.1, ECO:0000313|Proteomes:UP000178767};
RN [1] {ECO:0000313|EMBL:AOW92644.1, ECO:0000313|Proteomes:UP000178767}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WMMA185 {ECO:0000313|EMBL:AOW92644.1,
RC ECO:0000313|Proteomes:UP000178767};
RA Bugni T.S., Adnani N., Braun D., Chevrette M., McDonald B., Rajski S.;
RT "Draft Genome of Rhodococcus sp. WMMA185.";
RL Submitted (AUG-2016) 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; CP017014; AOW92644.1; -; Genomic_DNA.
DR RefSeq; WP_070378562.1; NZ_CP017014.1.
DR AlphaFoldDB; A0A1D8T4X9; -.
DR STRING; 679318.BFN03_07920; -.
DR KEGG; rhw:BFN03_07920; -.
DR OrthoDB; 9761717at2; -.
DR Proteomes; UP000178767; Chromosome.
DR GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro.
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; 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 Reference proteome {ECO:0000313|Proteomes:UP000178767}.
FT BINDING 46
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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 68
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 68
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 371
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 415
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 418
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 421
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
SQ SEQUENCE 430 AA; 48074 MW; 6C97F7799CB0AC91 CRC64;
MVPRNRELTV RALARVEGEG RVDVTVHDGR AERVELSIYE PPRFFESFLR GRHFLEPPDI
TSRICGICPV AYQVSACNAV EQACELVLDR SVLDLRRLLY CGEWIASHVL HIYFLHAPDF
FGVPDSIALA RHDREAVERG LALKKAGNAI LELIGGRPIH PVNVRIGGFH RTPTRAELGP
LADQLRTALD HAVATVEWVS AFEFPDIELD HDLVALHDDS RYAIEDGEIW SSSGLRCTAD
EFPHHVTEHQ VPHSTALHAE LDGRRYLAGP LARYSINSAQ LTDMAARTAT AAGLQGSCRN
PYRSIIIRAV EVVYAVEEAL RIIERYDRPM QPFIAGPPVR SVGHGVSEAP RGLLYHRYEL
DPTGLISAAS IIPPTSQNQA AIEYDLRRTV DENLTLTDDE LTALCERTIR NYDPCISCAT
HFLTLKIHRR
//
