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Database: UniProt
Entry: E3G894_ENTLS
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Original site: E3G894_ENTLS 
ID   E3G894_ENTLS            Unreviewed;      1071 AA.
AC   E3G894;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=Aldehyde oxidase and xanthine dehydrogenase molybdopterin binding protein {ECO:0000313|EMBL:ADO49762.1};
GN   OrderedLocusNames=Entcl_3518 {ECO:0000313|EMBL:ADO49762.1};
OS   Enterobacter lignolyticus (strain SCF1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Pluralibacter.
OX   NCBI_TaxID=701347 {ECO:0000313|EMBL:ADO49762.1, ECO:0000313|Proteomes:UP000006872};
RN   [1] {ECO:0000313|Proteomes:UP000006872}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCF1 {ECO:0000313|Proteomes:UP000006872};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N.,
RA   Mikhailova N., DeAngelis K., Arkin A.P., Chivian D., Edwards B., Woo H.,
RA   Hazen T.C., Woyke T.;
RT   "Complete sequence of Enterobacter cloacae SCF1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADO49762.1, ECO:0000313|Proteomes:UP000006872}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCF1 {ECO:0000313|EMBL:ADO49762.1,
RC   ECO:0000313|Proteomes:UP000006872};
RX   PubMed=22180812; DOI=10.4056/sigs.2104875;
RA   Deangelis K.M., D'Haeseleer P., Chivian D., Fortney J.L., Khudyakov J.,
RA   Simmons B., Woo H., Arkin A.P., Davenport K.W., Goodwin L., Chen A.,
RA   Ivanova N., Kyrpides N.C., Mavromatis K., Woyke T., Hazen T.C.;
RT   "Complete genome sequence of "Enterobacter lignolyticus" SCF1.";
RL   Stand. Genomic Sci. 5:69-85(2011).
CC   -!- COFACTOR:
CC       Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC         Evidence={ECO:0000256|ARBA:ARBA00001924};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|ARBA:ARBA00034078};
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DR   EMBL; CP002272; ADO49762.1; -; Genomic_DNA.
DR   RefSeq; WP_013367488.1; NC_014618.1.
DR   AlphaFoldDB; E3G894; -.
DR   STRING; 701347.Entcl_3518; -.
DR   KEGG; esc:Entcl_3518; -.
DR   eggNOG; COG1319; Bacteria.
DR   eggNOG; COG1529; Bacteria.
DR   HOGENOM; CLU_001681_2_3_6; -.
DR   Proteomes; UP000006872; Chromosome.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.90.1170.50; Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead; 1.
DR   Gene3D; 3.30.365.10; Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain; 4.
DR   Gene3D; 3.30.390.50; CO dehydrogenase flavoprotein, C-terminal domain; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
DR   InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
DR   InterPro; IPR016208; Ald_Oxase/xanthine_DH-like.
DR   InterPro; IPR008274; AldOxase/xan_DH_MoCoBD1.
DR   InterPro; IPR046867; AldOxase/xan_DH_MoCoBD2.
DR   InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
DR   InterPro; IPR005107; CO_DH_flav_C.
DR   InterPro; IPR036683; CO_DH_flav_C_dom_sf.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR   PANTHER; PTHR11908:SF132; ALDEHYDE OXIDASE 1-RELATED; 1.
DR   PANTHER; PTHR11908; XANTHINE DEHYDROGENASE; 1.
DR   Pfam; PF01315; Ald_Xan_dh_C; 1.
DR   Pfam; PF03450; CO_deh_flav_C; 1.
DR   Pfam; PF00941; FAD_binding_5; 1.
DR   Pfam; PF02738; MoCoBD_1; 1.
DR   Pfam; PF20256; MoCoBD_2; 1.
DR   SMART; SM01008; Ald_Xan_dh_C; 1.
DR   SMART; SM01092; CO_deh_flav_C; 1.
DR   SUPFAM; SSF55447; CO dehydrogenase flavoprotein C-terminal domain-like; 1.
DR   SUPFAM; SSF54665; CO dehydrogenase molybdoprotein N-domain-like; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF56003; Molybdenum cofactor-binding domain; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006872}.
FT   DOMAIN          782..957
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   1071 AA;  116637 MW;  CB0C7956F0802A63 CRC64;
     MCASRSAPLR RVDGLAKVKG TAIYGDDITL PGMLYGVCRF ADIPAGKIEE IDLSEALSVE
     GVVKIATWQD IPGTPAVGII VKDYLPIVKD EVVFHGDVVA VVAATSYEVA CEAADKIRVR
     YAPYVPLTDV EEAMAPDARR IHPECRDNVV AHHHTVKGDI EKGFAEAKHV IEREYEVGFQ
     EHAYIEPEVV LTWLDPTDGS LIISGSIQNP HRVRSFVAKF IGCPQSQINV KRAVMGGSFG
     GKDDIIDHLA CRSALMTRLT GCPVKFTYTR EQSIIESCKR HPYKMKYRAG MDDAGRILAI
     KIDILADSGG YAASSPFVTW RSSVQAAGPY NIPNVHIDVK AVYTNNSYTS AMRGFGSPQV
     VYANESFMDE IAETLNLSPV AVREVNALRQ GDTSVTGQLF DKHTVSAVEV LNKAVNASEF
     AARRQHYREL NLKGGVYRYG IGIALSYRGC SIGAEGVDTS TALIQVNEDG SVNLATSVSE
     NGQGLQTAMS LIAAETFGIE LADLHFMEPP TSVIGDGGST AATRGTMVGG GAILDAADKI
     KRRILSVVGD SIGTRELSET RWQNGFIINI QDSERRIDFK TAVNKTKWAS VSLTEYGWFV
     PPPIHWDEEK GCGSPYFTWV YGCQVAEVRV NTSTGKTDLL HVTAAHDVGR VLNPVGFEGQ
     VYGGVAQGFG YALLEDFNIE NGQVKSENFD SYLLPTMKDI PRMTVIGVEN PDIAGPLGAK
     GIGEPATELA AAAINNAVSF ALEARFNKLP LTLEQVILGY NLKKPVRQSE MMLEAENRKH
     VLRLTDVEVT RPQSLQEALT LLANDGVTAI AGGTDVIVQG RLQTRAMRLI DISHLPELTQ
     VSEDPATHEV TIGGAMTFNR ITDHPLLRER YPLLVQACHT VGSHQIRNRA TIGGNIVNAA
     PCGDSIPPAI LYDARIELCS LNGMRTLGLA EFLLSGYKTQ RQPDELLTKV ILPPPARPQA
     KGFYHQLGRR NALNITRQSL SALLDFADDG TVSYCRLVDG ALFSKPQRLL DIERCLLGKP
     LNSDSINSAC EVLDKLIYAA IGKRWSAAYK QPVFVNMFRD MMAEAQQVSG I
//
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