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Database: UniProt
Entry: A0Z936_9GAMM
LinkDB: A0Z936_9GAMM
Original site: A0Z936_9GAMM 
ID   A0Z936_9GAMM            Unreviewed;       367 AA.
AC   A0Z936;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   SubName: Full=Probable phenylacetic acid degradation NADH oxidoreductase {ECO:0000313|EMBL:EAW39554.1};
GN   ORFNames=MGP2080_12574 {ECO:0000313|EMBL:EAW39554.1};
OS   marine gamma proteobacterium HTCC2080.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae.
OX   NCBI_TaxID=247639 {ECO:0000313|EMBL:EAW39554.1, ECO:0000313|Proteomes:UP000004719};
RN   [1] {ECO:0000313|EMBL:EAW39554.1, ECO:0000313|Proteomes:UP000004719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2080 {ECO:0000313|EMBL:EAW39554.1,
RC   ECO:0000313|Proteomes:UP000004719};
RX   PubMed=20472793; DOI=10.1128/jb.00511-10;
RA   Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L.,
RA   Giovannoni S.J.;
RT   "Genome sequences of strains HTCC2148 and HTCC2080, belonging to the
RT   OM60/NOR5 clade of the Gammaproteobacteria.";
RL   J. Bacteriol. 192:3842-3843(2010).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:EAW39554.1}.
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DR   EMBL; AAVV01000017; EAW39554.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0Z936; -.
DR   eggNOG; COG1018; Bacteria.
DR   OrthoDB; 9796486at2; -.
DR   Proteomes; UP000004719; Unassembled WGS sequence.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd00207; fer2; 1.
DR   CDD; cd06214; PA_degradation_oxidoreductase_like; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR47354:SF8; 1,2-PHENYLACETYL-COA EPOXIDASE, SUBUNIT E; 1.
DR   PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00410; PHEHYDRXLASE.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   4: Predicted;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004719}.
FT   DOMAIN          4..108
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   DOMAIN          272..364
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   367 AA;  39815 MW;  75836129F5D76EDC CRC64;
     MSSSIFHPLK VASVVPETAH AVCLSFDVPA HLQDVFAFQP GQYLTLRTTI DDVPVSRAYS
     ICAPPSSQQL TVAIKRVDNG VFSNFANDHL QCGMTLEVMA PQGSFGLPTA EAIDTNYLFI
     AAGSGITPIM SMLTAALEAD PKATATLLYG NQRSSSIMFR QQLSFLKNQY LARFNWINIL
     SRETQDAPVL NGRIDNHKGA ELSRRVLNLK GFDGFFLCGP ESMISEVSRG LRDSGIPEDK
     IQYELFGSSA EDAAERVAKH HARAEAFSGK MCDVTLVNDG RASLVRIAAD GENLLDAGLN
     LGLDLPFACK GGVCSTCKAL LVEGEVEMDI QRGLTADEIA RGMILTCQAH PISERVHIDF
     DKRWSGA
//
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