ID A0A0Q9PYE8_9ACTN Unreviewed; 689 AA.
AC A0A0Q9PYE8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Nitrite reductase {ECO:0000313|EMBL:KRE95441.1};
GN ORFNames=ASG76_07275 {ECO:0000313|EMBL:KRE95441.1};
OS Nocardioides sp. Soil774.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736408 {ECO:0000313|EMBL:KRE95441.1, ECO:0000313|Proteomes:UP000051100};
RN [1] {ECO:0000313|EMBL:KRE95441.1, ECO:0000313|Proteomes:UP000051100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil774 {ECO:0000313|EMBL:KRE95441.1,
RC ECO:0000313|Proteomes:UP000051100};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE95441.1, ECO:0000313|Proteomes:UP000051100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil774 {ECO:0000313|EMBL:KRE95441.1,
RC ECO:0000313|Proteomes:UP000051100};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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:KRE95441.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMSM01000006; KRE95441.1; -; Genomic_DNA.
DR RefSeq; WP_056601925.1; NZ_LMSM01000006.1.
DR AlphaFoldDB; A0A0Q9PYE8; -.
DR STRING; 1736408.ASG76_07275; -.
DR OrthoDB; 7376058at2; -.
DR Proteomes; UP000051100; Unassembled WGS sequence.
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:InterPro.
DR CDD; cd00508; MopB_CT_Fdh-Nap-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:SF15; FORMATE DEHYDROGENASE H; 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 SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
PE 4: Predicted;
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}.
FT DOMAIN 1..52
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|SMART:SM00926"
SQ SEQUENCE 689 AA; 72982 MW; A621253B77C10DA4 CRC64;
MATETHCPYC SLQCGMRLAG RRVPEVQAWE EFPVNRGALC RKGWAAAGLY GSRERLTSPL
VRDRESGEWS AVSWDDALDR VAAGIRAAQA AKGPDGVAVF GGGGLTNEKA YSLGKLARAA
LGTSQIDYNG RWCMSSAASA GIRAFGLDRG LPFPLADVEE ADVLVLVGSN LAETMPPAAR
HLDRLRERGG RVVVIDPRRT PTADRADLVL QPVPGTDLAL ALGVLHLLVA AAAVDEDYLA
ARTTGWESVR DSVAGWWPER GERVTGIEAH ELRALAAMLA GSPKVMVLTA RGAEQHSTGS
DTVLAWINVA LALGMVGKRG AGYGCLTGQG NGQGGREHGQ KADQLPGYRR IDDPAARAHV
AGVWGVDPDT LPGPGRSAYE LLDALGTDDG PSALLVMGSN IVVSAPNATH VTSRLEALDL
LVVCDVVMSE TAAIADVVLP VTQWAEETGT MTNLEGRVVL RQKAITPPSG VRSDLDVIAG
LAARLSDVPF ATDPEEVFAE LGRASAGGPA DYSSITYDRI RDEGGVFWGG ERLFAETFAH
VDGRARMYAV EHRGAAEVPC ADYPVHLTTG RVLAQYQSGA QTRRTRALPD DGPFVELHPL
LAGRLGVAAG DPVRVATRRG SMAAPARVVT TIRPDTVFVP FHWVGANRLT NDALDPASRM
PEFKVCAASV ASLLEEVAQR PSRDPVTHA
//