ID V2U1T5_9GAMM Unreviewed; 1201 AA.
AC V2U1T5;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Urea carboxylase {ECO:0000313|EMBL:ESK48243.1};
GN ORFNames=P255_02886 {ECO:0000313|EMBL:ESK48243.1};
OS Acinetobacter brisouii CIP 110357.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1341683 {ECO:0000313|EMBL:ESK48243.1, ECO:0000313|Proteomes:UP000018418};
RN [1] {ECO:0000313|EMBL:ESK48243.1, ECO:0000313|Proteomes:UP000018418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 110357 {ECO:0000313|EMBL:ESK48243.1,
RC ECO:0000313|Proteomes:UP000018418};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Grillot-Courvalin C.,
RA Clermont D., Rocha E., Yoon E.-J., Nemec A., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Gnerre S., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter brisouii CIP 110357.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESK48243.1}.
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DR EMBL; AYEU01000012; ESK48243.1; -; Genomic_DNA.
DR RefSeq; WP_004898501.1; NZ_KI530765.1.
DR AlphaFoldDB; V2U1T5; -.
DR STRING; 396323.VH98_01200; -.
DR PATRIC; fig|1341683.3.peg.2856; -.
DR HOGENOM; CLU_002162_0_1_6; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000018418; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000018418}.
FT DOMAIN 1..443
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 1120..1198
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 1201 AA; 132755 MW; D410F9EC841C0F41 CRC64;
MFKKVLIANR GAIACRVIRT LKKLGIASVA VYSEADRDSL HVTLADEAFC IGAAPAQQSY
LNIEKIIEVA QQTGAEAIHP GYGFLSENAE FCDLCENQGI AFIGPNSSQM KDFGLKHTAR
ELAIKSKVPL LPGSSLLADQ AEALTEAARI GYPVMLKSTA GGGGIGMRLV WNESELKDAY
QTVSYLAQAN FKDAGLYLEK FVQHARHIEV QIFGDGQGQV LALGERDCSV QRRNQKVIEE
TPAPHLNNEQ RTYIQKVAIQ LMQSVNYRSA GTVEFVMDTE TQEFYFLEVN TRLQVEHGVT
EQVFGVDLVE WMVTLASGDW TAPTEELAPK GHSIQVRLYA EDPIKQFQPS AGLLTYVKFD
EQARVETWVE TGSNVSSFYD PMIAKIIVTA HTRDEAIQAM SSSLKKTKVA GIETNLEYLQ
NIIACDVFHE GTQTTRFLNT FEWKTQKIEV LQAGIQTSVQ DVTGRLGYWD VGVPPSGAID
PLSLTVANQL LGNPKNTAGL ECTLQGPTLK FHCDSQIVIT GGDMPSKLDG EAVPMWQTIN
VKKGQVLKCG SITTGCRSYI GIKGGLDVPE YLGSQATFTL GQFGGHAGRN LLIGDMLPIT
EYLTQSTTAL PQAQIPQFAH TWEIAVMYGP HGAPDFFTKQ DIDTFFANAF EIHYNSSRTG
IRLIGPKPEW ARQDGGEAGL HPSNIHDNAY AIGAIDFTGD MPIILGPDGP SLGGFVCPAV
VIHSELWKIG QLKAGDKVKF IPVSYAQAKA LDQQYHQSVM ADDVSGIDFS PEFNAETEAL
NDAVLATLAG QDDLPSVTYR PAGNSYLLVE YGELVLDLNL RFRIHALMQW VKDQDIQGII
DLTPGIRSLQ IHFDSIELDQ IELLHKLQQA ENELPDIHNM QVPSRTVYLP LAWEDSQTQL
ATERYTQIVR PDAPWCPDNV EFIRRINGLA SKQAVKDVVY SANYLVMGLG DVYLGAPVAT
PLDPRQRLVT TKYNPARTWT PENAVGIGGA YMCVYGMEGP GGYQFVGRTT QMWSRYRKNV
DFEDGKPWLL RFFDQVKFYE VSEAELLHMR EDFKAGRLKL RIEDGVLNLK EYNDFLEKNA
ETIHAFKDMQ QANFEAERRR WHEAGLQEYV SESLDAVDDG EAVTIPEGGC SVESHMPGSI
WKIECALGDI VEEGATLAVI EAMKIEIPIV APERMKVEAI TIEKGQTVKT GQVLFTLAPV
A
//
