ID L0DKJ2_SINAD Unreviewed; 763 AA.
AC L0DKJ2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Putative anaerobic dehydrogenase {ECO:0000313|EMBL:AGA29879.1};
GN OrderedLocusNames=Sinac_5749 {ECO:0000313|EMBL:AGA29879.1};
OS Singulisphaera acidiphila (strain ATCC BAA-1392 / DSM 18658 / VKM B-2454 /
OS MOB10).
OC Bacteria; Planctomycetota; Planctomycetia; Isosphaerales; Isosphaeraceae;
OC Singulisphaera.
OX NCBI_TaxID=886293 {ECO:0000313|EMBL:AGA29879.1, ECO:0000313|Proteomes:UP000010798};
RN [1] {ECO:0000313|EMBL:AGA29879.1, ECO:0000313|Proteomes:UP000010798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1392 / DSM 18658 / VKM B-2454 / MOB10
RC {ECO:0000313|Proteomes:UP000010798};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Chertkov O.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Tindall B., Pomrenke H., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "Complete sequence of chromosome of Singulisphaera acidiphila DSM 18658.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- PATHWAY: Nitrogen metabolism. {ECO:0000256|ARBA:ARBA00004909}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. NasA/NapA/NarB subfamily.
CC {ECO:0000256|ARBA:ARBA00008747}.
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DR EMBL; CP003364; AGA29879.1; -; Genomic_DNA.
DR RefSeq; WP_015248976.1; NZ_JH621486.1.
DR AlphaFoldDB; L0DKJ2; -.
DR STRING; 886293.Sinac_5749; -.
DR KEGG; saci:Sinac_5749; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_4_0; -.
DR OrthoDB; 9805142at2; -.
DR Proteomes; UP000010798; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd00508; MopB_CT_Fdh-Nap-like; 1.
DR CDD; cd02754; MopB_Nitrate-R-NapA-like; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR PANTHER; PTHR43105:SF9; NITRATE REDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G15190)-RELATED; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR PIRSF; PIRSF000144; CbbBc; 2.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000010798}.
FT DOMAIN 45..101
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 733..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 763 AA; 84194 MW; 25EA5C23C908A718 CRC64;
MTAAHTILNK LRSLVRARDG ILTQELLRTP GKFGLGQVPA LKAPDATTGV VCGYCSTGCG
LTVHLREGEA VNLSPSADYP VNLGMACPKG WEALTVLEAD DRATTPLLRG DDGIRRPVDW
HTAMETFAAR FKSIQAEHGN ESVAYLSTGQ IATEEMALLG AVAKFGMGIK HGDGNTRQCM
ATAVVAYKQA FGFDAPPYTY QDFEESDCIV LVGSNLCIAH PIMWERVMKN RNAPEIVVVD
PRRTETAVSA TLHLQARPKT DLVLFYGLAN LMIERGWVDR SFVEAHTSGF DDYARFVRRF
GLLSVAYETG LEAQQIEHLA ELIHRKKRVS FWWTMGVNQS HEGVRTAQAI INLALLTGNI
GRPGTGANSI TGQCNAMGSR LFSNTTNLLG GHDFADPLHR SKVAGVLEIP EDRIPTQAGW
TYDRIVDGIR EGKIRGLWVI ATNPAHSWIH QQDFRQLLGT LDFLVVQDMY SSTETALAAD
LLLPAAGWGE KEGTFINSER RVGLIKKVRR APGQALSDFH IFKLAAHYYG CGEMFKRWES
PESIFQILKA LSANQPCDFT GIRDYRSLDE ARGIQWPYPE GAADLSSQRR LFADGRFYHA
DGRARFVFEN PRPMGESPDD EYPFLLLTGR GSASQWHTQT RTAKSGVLRK LYPAELHAEI
HPADARWLGI GPGQAMIVES RRGRVHAKAF VTPTVGQGQV FLPMHDPVTN TLTYPDFDPN
SRQPAYKGCA VRIRSEGPGA PPESVRSDRP LQAGNVGTER VRS
//