ID N9P0E7_9GAMM Unreviewed; 1201 AA.
AC N9P0E7;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Urea carboxylase {ECO:0000313|EMBL:ENX08402.1};
GN ORFNames=F897_02163 {ECO:0000313|EMBL:ENX08402.1};
OS Acinetobacter variabilis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=70346 {ECO:0000313|EMBL:ENX08402.1, ECO:0000313|Proteomes:UP000013101};
RN [1] {ECO:0000313|EMBL:ENX08402.1, ECO:0000313|Proteomes:UP000013101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIPH 2171 {ECO:0000313|EMBL:ENX08402.1,
RC ECO:0000313|Proteomes:UP000013101};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter sp. NIPH 2171.";
RL Submitted (FEB-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:ENX08402.1}.
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DR EMBL; APRS01000013; ENX08402.1; -; Genomic_DNA.
DR RefSeq; WP_005235754.1; NZ_KB850113.1.
DR AlphaFoldDB; N9P0E7; -.
DR STRING; 70346.F897_02163; -.
DR PATRIC; fig|1217693.3.peg.2091; -.
DR HOGENOM; CLU_002162_0_1_6; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000013101; 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}.
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; 132630 MW; 3D6FEEE703C7F0BE CRC64;
MFNKVLIANR GAIACRVIRT LKKLGIQSVA VYSEADRDSL HVTLADEAVY IGEAPASQSY
LNVDKILEVA KQTGAQAIHP GYGFLSENAE FCDLCESQGI AFIGPNSAQM RAFGLKHTAR
ELAIQANVPL LPGSQLLADE AEALTEANRI GYPVMLKSTA GGGGIGMRLV WNEAELKDAY
ATVSYLAQAN FKDAGLYLEK FVQNARHIEV QIFGDGQGKV IALGERDCSV QRRNQKVIEE
TPAPHINDVQ RAYIQNVAIQ LMESVNYRSA GTVEFVMDTD TQEFYFLEVN TRLQVEHGVT
EQVFSVDLVE WMVTLASGDW TAPTAQLESK GHSIQVRLYA EDPIKNFQPS AGLLTYVEFD
DKARNETWVE TGSNVSSFYD PMIAKIIVTA DDRESAIQAM SDTLAKTQVA GIETNLEYLQ
NIIDCDVFKS GTQTTRFLNT FDWKTQKIEV LQAGIQTAVQ DVTGRLGYWD VGVPPSGAID
PLSLNVANQL LGNVPNTAGL ECTLQGPSLK FHCDSQIVLA GGDMPSSLDG VSVPMWQTVN
VRKGQVLKCG KIATGCRTYI GIKGGLNVPE YLGSQATFTL GQFGGHAGRN LLIGDMLPIT
AFTSDDVKAL SEDQIPAFSN SWEIAVMYGP HGAPDFFTKN DIDTFFANEF EIHFNSSRTG
IRLIGPKPEW ARQDGGEAGL HPSNIHDNAY AIGAIDFTGD MPIILGPDGP SLGGFVCPAV
VINSELWKLG QLKAGDKVKF VPVSYHQAKL LNEKYHAQLT AVDTQAVIFD ESFYPEISTL
KSAILDTLKG QNGTPDVVYR PAGNNYMLVE YGELVLDLNL RFRIHALMQW VKDQNIQGII
DLTPGIRSLQ IHFDSTQLDQ IDLLRMLQVA EEQLPDVTEM QVPSRTVYLP LAWEDSQTQL
ATERYMQTVR PDAPWCPDNI EFIRRINGLK DKQAVKDVVY NASYLVMGLG DVYLGAPVAT
PLDPRQRLVT TKYNPARTWT PENAVGIGGA YMCVYGMEGP GGYQFVGRTS QMWSRYRKNP
DFEQGMPWLL RFFDQIKFYE VSEAELMHMR EDFKAGRLKL RIEDGVLNLK EYNDFLTEHQ
ESISAFKAVQ QANFDSERRR WHEAGLAEYV SESLDAVDDG EGVEVPEGGC AVESHMPGSI
WKIECQSGDI VEEGATLAVI EAMKIEIPII APERMRVDAI TIEKGQTVKT GQVLFTLAPV
A
//
