ID B3PBF6_CELJU Unreviewed; 1205 AA.
AC B3PBF6;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Urea amidolyase homolog {ECO:0000313|EMBL:ACE84124.1};
DE EC=3.5.1.54 {ECO:0000313|EMBL:ACE84124.1};
GN OrderedLocusNames=CJA_2723 {ECO:0000313|EMBL:ACE84124.1};
OS Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS cellulosa).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=498211 {ECO:0000313|EMBL:ACE84124.1, ECO:0000313|Proteomes:UP000001036};
RN [1] {ECO:0000313|EMBL:ACE84124.1, ECO:0000313|Proteomes:UP000001036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ueda107 {ECO:0000313|EMBL:ACE84124.1,
RC ECO:0000313|Proteomes:UP000001036};
RX PubMed=18556790; DOI=10.1128/JB.01701-07;
RA Deboy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA Nelson K.E.;
RT "Insights into plant cell wall degradation from the genome sequence of the
RT soil bacterium Cellvibrio japonicus.";
RL J. Bacteriol. 190:5455-5463(2008).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; CP000934; ACE84124.1; -; Genomic_DNA.
DR RefSeq; WP_012488317.1; NC_010995.1.
DR AlphaFoldDB; B3PBF6; -.
DR STRING; 498211.CJA_2723; -.
DR KEGG; cja:CJA_2723; -.
DR eggNOG; COG0439; Bacteria.
DR eggNOG; COG1984; Bacteria.
DR eggNOG; COG2049; Bacteria.
DR eggNOG; COG4770; Bacteria.
DR HOGENOM; CLU_002162_3_1_6; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000001036; Chromosome.
DR GO; GO:0004039; F:allophanate hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.1360.40; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 2.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR003778; CT_A_B.
DR InterPro; IPR003833; CT_C_D.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR InterPro; IPR014084; Urea_COase.
DR NCBIfam; TIGR00724; urea_amlyse_rel; 1.
DR NCBIfam; TIGR02712; urea_carbox; 1.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR Pfam; PF02626; CT_A_B; 1.
DR Pfam; PF02682; CT_C_D; 1.
DR SMART; SM00796; AHS1; 1.
DR SMART; SM00797; AHS2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF50891; Cyclophilin-like; 2.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF160467; PH0987 N-terminal domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ACE84124.1};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Lyase {ECO:0000313|EMBL:ACE84124.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000001036}.
FT DOMAIN 1..449
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1126..1204
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 1205 AA; 132721 MW; 60BEF69091F6F961 CRC64;
MFAKVLVANR GAIATRIIRT LKKLNIHAIA IYAESDADSL HVRLADEAWS LGEGAAAHTY
LDRQKIIAIA RQTGAQAIHP GYGFLSENAS FVAECEAADI VFIGPTAEQM ITFGLKHKAR
ELAQAAGVPL CPGTDLLPSL EDATQAANCI GYPVMLKSTA GGGGIGMQLC HSDSELIAAF
DSVKRLGKNN FADDGVFLEK FIAAARHIEV QVFGDGQGTA VAIGERDCSS QRRNQKVVEE
CPAPNLPEAQ RQAMQQVAEQ LLASVCYRNA GTVEFIYDSL DNRFYFLEVN TRLQVEHGVT
EEVYSVDLVE WMLKQAAGEL GNLRALRAPL SPRGHAIQVR VYAEDPVLNF QPCAGLLSKV
EFPATSDQVR IDHWIESGIE VPAYFDPMLA KIIVKGDNRT QALARLDNTL AHTHIYGIET
NLGYLRRLLQ DDTLVQGKMT TRYLNHFIYQ APRIDVLQGG TQTTIQDYPG RQGYWHVGVP
TSGPFDSYSF RLGNRLLNNP QTAAGLEITL QGPLLKFGGA THIVITGAAI EAKLDGKPLS
LNQVHAINAG QQLHLGRITT GARAYLCVAG GIQCPDYLGA KSTFTLGQFG GHNGRALRAG
DVLALSHDTA LLAADTGNLA TDTTLPDDLL PTIGNHWELR VIYGPHGAPD FFTDRDINTF
FATDWEVHYN SSRTGVRLIG PKPEWARSSG GEAGMHPSNI HDNAYAFGTV DFTGDMPVIL
GPDGPSLGGF VCPATVITAD LWKLGQVRAG DKIRFVPIAI EDAVALEKAQ CHTLHSLTAR
PHDYQPVVPD TPIVQTLPAE EFGEDIVYRV AGDHFLLVEY GPLELDIQLR FRAHALMQWL
EKNSLPGLRE LTPGIRSLQI HYDSQQLALP LLLAHLKQAE QALITQLAEL RVPSRIVHLP
LSWDDEACQI AIQKYMQSVR ANAPWCPSNL EFIRRINGLD SIEAVKDIVF NASYLVMGLG
DVYLGAPVAT PVDPRHRLVT TKYNPARTWT AENSVGIGGS YLCIYGMEGP GGYQFVGRTL
QMWNRYRKTR EFQQPWLLNF FDQIRFYPVS AEELQRIRRD FPQGRYNITI EDSSFSLSEY
QHFIDQQADS INNFKHQREQ AFDQELARWH ANGQFNYEQA EIVEDSEETE LPEDAIRIDS
SVSGSVWQTQ VKVGQAVNAG DILLILESMK MEINITAPCA GTVTHLLKTD GARVQAGQTL
VVLGN
//