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
//