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Database: UniProt
Entry: A8SZR3_9VIBR
LinkDB: A8SZR3_9VIBR
Original site: A8SZR3_9VIBR 
ID   A8SZR3_9VIBR            Unreviewed;       605 AA.
AC   A8SZR3;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   SubName: Full=Dihydroorotase {ECO:0000313|EMBL:EDP60499.1};
DE            EC=3.5.2.3 {ECO:0000313|EMBL:EDP60499.1};
GN   ORFNames=AND4_06264 {ECO:0000313|EMBL:EDP60499.1};
OS   Vibrio sp. AND4.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=314289 {ECO:0000313|EMBL:EDP60499.1, ECO:0000313|Proteomes:UP000005159};
RN   [1] {ECO:0000313|EMBL:EDP60499.1, ECO:0000313|Proteomes:UP000005159}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AND4 {ECO:0000313|EMBL:EDP60499.1,
RC   ECO:0000313|Proteomes:UP000005159};
RX   PubMed=20436956; DOI=10.1371/journal.pbio.1000358;
RA   Gomez-Consarnau L., Akram N., Lindell K., Pedersen A., Neutze R.,
RA   Milton D.L., Gonzalez J.M., Pinhassi J.;
RT   "Proteorhodopsin phototrophy promotes survival of marine bacteria during
RT   starvation.";
RL   PLoS Biol. 8:E1000358-E1000358(2010).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|ARBA:ARBA00034078};
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:EDP60499.1}.
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DR   EMBL; ABGR01000001; EDP60499.1; -; Genomic_DNA.
DR   RefSeq; WP_009840957.1; NZ_ABGR01000001.1.
DR   AlphaFoldDB; A8SZR3; -.
DR   OrthoDB; 581532at2; -.
DR   Proteomes; UP000005159; Unassembled WGS sequence.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0004151; F:dihydroorotase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   CDD; cd00207; fer2; 1.
DR   CDD; cd06215; FNR_iron_sulfur_binding_1; 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; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR005302; MoCF_Sase_C.
DR   InterPro; IPR005303; MOCOS_middle.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR   PANTHER; PTHR47354:SF6; NADH OXIDOREDUCTASE HCR; 1.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF03473; MOSC; 1.
DR   Pfam; PF03476; MOSC_N; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00406; CYTB5RDTASE.
DR   PRINTS; PR00371; FPNCR.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF141673; MOSC N-terminal domain-like; 1.
DR   SUPFAM; SSF50800; PK beta-barrel domain-like; 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.
DR   PROSITE; PS51340; MOSC; 1.
PE   4: Predicted;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW   Hydrolase {ECO:0000313|EMBL:EDP60499.1};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Membrane {ECO:0000256|ARBA:ARBA00022692};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692}.
FT   DOMAIN          113..264
FT                   /note="MOSC"
FT                   /evidence="ECO:0000259|PROSITE:PS51340"
FT   DOMAIN          277..380
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   DOMAIN          521..605
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   605 AA;  67487 MW;  FEDC02B0C6C46000 CRC64;
     MSQSVLSQIN VFPVKSVGGV SLSSAWVEKQ GLSFDRRFMI ATSDGSMVTA RKFPQMVTIK
     SALLPDGVVF TSLGEEPLTI RYQDFKMQEA PATVWKDSFT AYTTTDEADD WFSKVLGLRV
     ELLFTGEQSN RVRDKLGHNV SFADGYPVLV ISEASLEELN RRSAEQHSMD QFRTNLVVSD
     TTPFEEDTWK RIRIGEVEFE SVKPCERCIL TTVNTQRGTF RESKEPLKTL QEFRANERGG
     VFFGQNLVAL NQGIIRSGDH VEVLEYKEPE FYPDNSPKRM TLTCVEREEI ARDFVTLWLE
     PREGQLPTYL PGQHLPIVVE VDGQTIGRRY TLSSSPSRPG RYAISVKRVS GGRVSNALLD
     NLQIGDVLEA ETPDGQFHLK AHAVQPLLLM SAGSGVTPML SMVRYLADHN QLDDVVFYHQ
     CSSEIDIPCK DELNELKRQN PGLDVKICLT QPSIDWFGLK GRVSLSHIKQ IKDVEHRQVF
     VCGPDGFMQK AKNLLLKKGL PEGNYHQEAF GVAMAAAKPE KSVEIEFNGV KWMGNNQQTL
     LEQVENAGKH ITNSCRAGLC GACEVQLESG LVDHPDLPAL SAEERAMGKV LACCAIPQTD
     VTLKD
//
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