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Database: UniProt/TrEMBL
Entry: D2TP31_CITRI
LinkDB: D2TP31_CITRI
Original site: D2TP31_CITRI 
ID   D2TP31_CITRI            Unreviewed;      1071 AA.
AC   D2TP31;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   01-MAY-2013, entry version 22.
DE   SubName: Full=Uncharacterized protein;
GN   OrderedLocusNames=ROD_33881;
OS   Citrobacter rodentium (strain ICC168) (Citrobacter freundii biotype
OS   4280).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=637910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ICC168;
RX   PubMed=19897651; DOI=10.1128/JB.01144-09;
RA   Petty N.K., Bulgin R., Crepin V.F., Cerdeno-Tarraga A.M.,
RA   Schroeder G.N., Quail M.A., Lennard N., Corton C., Barron A.,
RA   Clark L., Toribio A.L., Parkhill J., Dougan G., Frankel G.,
RA   Thomson N.R.;
RT   "The Citrobacter rodentium genome sequence reveals convergent
RT   evolution with human pathogenic Escherichia coli.";
RL   J. Bacteriol. 192:525-538(2010).
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DR   EMBL; FN543502; CBG90102.1; -; Genomic_DNA.
DR   RefSeq; YP_003366851.1; NC_013716.1.
DR   EnsemblBacteria; CBG90102; CBG90102; ROD_33881.
DR   GeneID; 8711769; -.
DR   KEGG; cro:ROD_33881; -.
DR   PATRIC; 32030474; VBICitRod33214_3223.
DR   HOGENOM; HOG000244715; -.
DR   BioCyc; CROD637910:GJIG-3414-MONOMER; -.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0008762; F:UDP-N-acetylmuramate dehydrogenase activity; IEA:InterPro.
DR   Gene3D; 3.30.365.10; -; 6.
DR   Gene3D; 3.30.43.10; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.90.1170.50; -; 1.
DR   InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
DR   InterPro; IPR008274; AldOxase/xan_DH_Mopterin-bd.
DR   InterPro; IPR005107; CO_DH_flav_C.
DR   InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2.
DR   InterPro; IPR016166; FAD-bd_2.
DR   InterPro; IPR016167; FAD-bd_2_sub1.
DR   InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR   Pfam; PF01315; Ald_Xan_dh_C; 1.
DR   Pfam; PF02738; Ald_Xan_dh_C2; 1.
DR   Pfam; PF03450; CO_deh_flav_C; 1.
DR   Pfam; PF00941; FAD_binding_5; 1.
DR   SMART; SM01008; Ald_Xan_dh_C; 1.
DR   SMART; SM01092; CO_deh_flav_C; 1.
DR   SUPFAM; SSF56003; Ald_xan_DH_mo_bd; 1.
DR   SUPFAM; SSF54665; Aldxan_dh_hamm; 1.
DR   SUPFAM; SSF55447; CO_deh_flav_C; 1.
DR   SUPFAM; SSF56176; FAD-binding_2; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   Complete proteome.
SQ   SEQUENCE   1071 AA;  116707 MW;  BBF0A193795E5D9F CRC64;
     MDTLLVGNEV PRVDGLAKVT GKAVYGDDIK MKDMLYGVCR YVDIAAGHID ALDLTEAEKV
     PGVVCIATWD DIPGQRKLGA IIPDHPPIID KEIAYRGDVI AVVAAESYEA ACVAVEKIKV
     TYTPWEPITS PEEAMKPGAR LIHSELDSNI INRHHTVKGD IDAGFAASTH IFEREYEVGF
     QEHGYIEPES IIAYLDDNEQ IMTIAGSIQN AHRTRAVVAK YLNIPQAKVN VKRSVLGGSF
     GGKDDIIDNV SCRAALLVHL TGRPVKISYN REQSMRESYK RHPYKMKYRI GLDDDARIQA
     IKIEIIADGG SYSGQTMFVT WRSSVQAAGP YNIPNVRVDL VGVYTNNNYT SAYRGYGAPQ
     VIFANESLMD EVAEQMGLSP VELRLRNVLK QGDTSMAGQV FDGHTVSARE VLEKSLIKAE
     YEARRAHYQQ LNAKGGPIRY GIGFALSHRG CSLGAEGLDA SSALIQVNAD GSINISTSVS
     ENGQGLQTTM SLLAAEAFGV GLDRVMFTEP ATAMIADGGS TVASRGTLMG GQAILNAANK
     IKKRMAEAVK ETLQAEGPDD LAWQEGKVFN RHRPELGLSF QQVVDMTKAT GANLSSYGWH
     VAPDIHWDEE KGCGNPYFTW VYGCQLADVA VDMRTGKVTV NNVVATHDVG KVINPVGFSG
     QVYGGVLQGM IGYGMLEDFN TESGVVKSEN FDTYLLPTIK DMPHIDIIAV ENYDKAGPMG
     AKVIGEPVLE LGAAALNNAV SFAIGRRNRT LPLTLEQVRL GYNLKKPERQ SEQMLDAGEK
     KQVHRLNTLS LSMPQTLEQA LTLLAEKGAM PIAGGTDVLV QARMQSGEVP LVNIAALAEL
     KEITDNNGGV SIGAGVCFTD LVRHPLISQR YPLLVTACKT IGSLQLRNRA TIGGNIVNAA
     PCADSMPPLI IYDAEIELRS LRGTRRMLVS EFVTGGYRTC LEPDELVTKF ILPAPVKQPL
     SNHYLQLGRR NALNITRQSL TGQFHVDKDN VIRLCRLVDG ALMSKPQRLL EVEQALTGKV
     LNAETVNQAA QVLNGLVEKA IGGRWSAPYK IPVFLDMFRQ MLQDVMTEQS K
//
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