ID N8WIV1_9GAMM Unreviewed; 1201 AA.
AC N8WIV1;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Urea carboxylase {ECO:0000313|EMBL:ENU96813.1};
GN ORFNames=F970_00344 {ECO:0000313|EMBL:ENU96813.1};
OS Acinetobacter sp. CIP 102082.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1144663 {ECO:0000313|EMBL:ENU96813.1, ECO:0000313|Proteomes:UP000018448};
RN [1] {ECO:0000313|EMBL:ENU96813.1, ECO:0000313|Proteomes:UP000018448}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 102082 {ECO:0000313|EMBL:ENU96813.1,
RC ECO:0000313|Proteomes:UP000018448};
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. CIP 102082.";
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:ENU96813.1}.
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DR EMBL; APPD01000030; ENU96813.1; -; Genomic_DNA.
DR RefSeq; WP_004680876.1; NZ_KB849371.1.
DR AlphaFoldDB; N8WIV1; -.
DR PATRIC; fig|1144663.3.peg.327; -.
DR HOGENOM; CLU_002162_0_1_6; -.
DR Proteomes; UP000018448; 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; 133104 MW; 267D7E592AA64F93 CRC64;
MFNKVLIANR GAIACRIIRT LKKLGIQSVA VYSEADRDSL HVTLADEAVF IGDSAAQQSY
LNIDKILEVA KQTGAQAIHP GYGFLSENAT FCDLCEQQGI VFIGPTSQQM RDFGLKHTAR
ELAIENNVPL LPGSQLLKDE AEAIAEASRI GYPVMLKSTA GGGGIGMRLV WNETELQEAY
QTVSYLAQAN FKDAGLYLEK FVQNARHIEV QIFGDGQGKV LALGERDCSV QRRNQKVIEE
TPAPHLNAEQ REYIQKVAIQ LMQSVQYRSA GTVEFVMDTD TQQFYFLEVN TRLQVEHGVT
EQVFGLDLVE WMVTLASGDW VAPTELSEPK GHSIQVRLYA EDPIKNFQPS AGLLTSVQFD
ADSRVETWVE TGSNVSSFYD PMIAKIIVTA VDREQAIQAM QNSLSNTEIA GIETNLEYLQ
NIVGCDVFHA GTQTTRFLNS FEWKTEKVEV LQAGIQTAVQ DVTGRLGYWD VGVPPSGAMD
ALSLNVANQL LGNPFNTAAL ECTLQGPTLK FHCDSQIALT GGHMQVTLDG VDVPMWTTIN
IRKGQVLKCG RIITGCRSYI GIKNGLKLPD YLGSQATFTL GQFGGYAGRN LLIGDMLPIS
AYHSTETTTL EPAQIPDFTQ TWQIAVMYGP HGAPDFFTAQ DISMFFAQEW EIHFNSSRTG
IRLVGPKPEW ARIDGGEAGL HPSNIHDNAY AIGAIDFTGD MPIILGPDGP SLGGFVCPAV
VIHSELWKLG QLKAGDKVQF IPVSYQQAQQ LEQRYQAALQ SKNTAQVNFS AAIHAEPITL
KNAVLATLQQ GADKPNVTYR PAGNQYLLVE YGDLVLDLNL RFRIHALMQW VKSQNIQGII
DLTPGIRSLQ IHFDSSVLDQ LDLLRLLQVA EAELPDIENM QVPSRTVYLP LAWEDSQTQL
ATEKYIQLVR PDAPWCPDNI EFIRRINGLS SKQAVKDIVY STSYLVMGLG DVYLGAPVAT
PLDPRHRLVT TKYNPARTWT PENAVGIGGA YMCVYGMEGP GGYQFVGRTT QVWSRYRQNP
NFEQHKPWLL RFFDQIKFYE VSESELMAMR EDFKAGRLQL KIEEGVLNLK EYNAFLQENQ
DSIQAFKQVQ QSNFEAERQR WHEAGLAEYV SEALDIIVDD SEINIPNGGM VVESHMPGSV
WKIECAVGDV IEEGQTLAVI EAMKIEIPIV APAKMQVDQI LIDKAQTVKT GQVLFTLAPV
A
//
