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Database: UniProt
Entry: Q6D5X1_PECAS
LinkDB: Q6D5X1_PECAS
Original site: Q6D5X1_PECAS 
ID   Q6D5X1_PECAS            Unreviewed;      1200 AA.
AC   Q6D5X1;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   24-JAN-2024, entry version 110.
DE   SubName: Full=Allophanate hydrolase {ECO:0000313|EMBL:CAG74820.1};
DE            EC=3.5.1.54 {ECO:0000313|EMBL:CAG74820.1};
GN   OrderedLocusNames=ECA1917 {ECO:0000313|EMBL:CAG74820.1};
OS   Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS   carotovora subsp. atroseptica).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=218491 {ECO:0000313|EMBL:CAG74820.1, ECO:0000313|Proteomes:UP000007966};
RN   [1] {ECO:0000313|EMBL:CAG74820.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SCRI1043 {ECO:0000313|EMBL:CAG74820.1};
RA   Bell K.S., Sebaihia M., Pritchard L., Holden M., Hyman L.J., Holeva M.C.,
RA   Thomson N.R., Bentley S.D., Churcher C., Mungall K., Atkin R., Bason N.,
RA   Brooks K., Chillingworth T., Clark K., Doggett J., Fraser A., Hance Z.,
RA   Hauser H., Jagels K., Moule S., Norbertczak H., Ormond D., Price C.,
RA   Quail M.A., Sanders M., Walker D., Whitehead S., Salmond G.P.C.,
RA   Birch P.R.J., Barrell B.G., Parkhill J., Toth I.K.;
RT   "The genome sequence of the enterobacterial phytopathogen Erwinia
RT   carotovora subsp. atroseptica SCRI1043 and functional genomic
RT   identification of novel virulence factors.";
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR   EMBL; BX950851; CAG74820.1; -; Genomic_DNA.
DR   RefSeq; WP_011093485.1; NC_004547.2.
DR   AlphaFoldDB; Q6D5X1; -.
DR   STRING; 218491.ECA1917; -.
DR   KEGG; eca:ECA1917; -.
DR   PATRIC; fig|218491.5.peg.1949; -.
DR   eggNOG; COG0439; Bacteria.
DR   eggNOG; COG1984; Bacteria.
DR   eggNOG; COG2049; Bacteria.
DR   HOGENOM; CLU_002162_3_0_6; -.
DR   OMA; TLQMWNR; -.
DR   OrthoDB; 9763189at2; -.
DR   Proteomes; UP000007966; 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: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:CAG74820.1};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000007966}.
FT   DOMAIN          1..450
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..1197
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   1200 AA;  130949 MW;  DCB6B03600414C48 CRC64;
     MFDTLLIANR GAIACRILRS LREMNVRGVA VYSDADISSL HIQDADEAIS LGEGAAAHTY
     LDVAKILSAA QRSGAQAIHP GYGFLSENAA FAEACETAQI AFVGPTPQQL RVFGLKHTAR
     ALAKKYHVPL LEGTELLENI DAALCAAAEI GYPVMLKSTA GGGGIGMRVC YSATELSEAF
     ETVKRLGQNN FSDAGVFIEK YIERARHLEV QIFGDGQGEV LALGVRDCSV QRRNQKVIEE
     TPAPNLPDGV ADALCSAAIS LAQAVNYRSA GTVEFVYDSA TDRFYFLEVN TRLQVEHGVT
     EQVWGVDLVR WMIELAAGDL PPLRELAAQL NPQGHAIQAR LYAEDPGKQF QPSPGLLTEV
     EFPVSEGHSL RIDTWVTAGC DIPPFFDPML AKIIACAPTR EQAMVELDRA LADTRLYGVE
     HNRDYLRQIL AAEPFASGQP WTRCLDALAY KATTCEVVSA GTQTTVQDYP GRLGYWSVGV
     PPSGPMDDRA LRLGNRLVGN PAGTAALEVT MNGPTLRFNT DAVAVVTGAA IAIEMGGQPI
     PMDRVFAIPT GATLRLGAMQ KQGVRSYLCL RGGIEVPDYL GSKSTFTLGQ FGGHAGRALR
     AGDVLHLAPL EDKRVGDSLP DALCTTLSTV RELRVIYGPH AAPDYFTPAY MDTFLTTEWE
     VHFNSSRTGV RLIGPKPEWV RDSGGEAGLH PSNIHDNPYA IGAVDFTGDM PVILGPDGPS
     LGGFVCPVTV IEADLWALGQ LNAGDRVRFI PVDLTTARSL ALACHAEVEQ LAPINIDWSP
     AALISPVVLD IGDADKRLVA RLSGDTHLLL EVGAAELDVA LRFRVHALML ALEQQTLDGI
     IDITPGIRSL QVHYRPETLA LSPLLEVLSS LWLTVCAQQN LTVPSRVVYL PLSWDDPACQ
     LAIQKYMTTV RSDAPWCPSN LEFIRRINEL DNLDEVYRTV FEASYLVMGL GDVYLGAPVA
     TPLDPRHRLV TTKYNPARTW TAENSVGIGG AYLCVYGMEG PGGYQFVGRT LQMWDRYRGV
     DAFDGKPWLL RFFDQIRFYP VSADELLSIR RDFPLGRYPL RIEQSELVLS AYQDFLSREA
     EDIETFRVRQ RAAFEAERER WRIAGQSVSD SVDVVIEETS ETPIQPGQIG VESPISGNLW
     QVETEVGDTV AEGETLMILE SMKMEIPIVS PQRGIVRDIR CQPGASVRAG QCVVVIEYQG
//
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