ID D4XQM3_ACIHA Unreviewed; 1206 AA.
AC D4XQM3;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE SubName: Full=Urea carboxylase {ECO:0000313|EMBL:EFF82509.1};
DE EC=6.3.4.6 {ECO:0000313|EMBL:EFF82509.1};
GN Name=uca {ECO:0000313|EMBL:EFF82509.1};
GN ORFNames=HMP0015_2015 {ECO:0000313|EMBL:EFF82509.1};
OS Acinetobacter haemolyticus ATCC 19194.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=707232 {ECO:0000313|EMBL:EFF82509.1, ECO:0000313|Proteomes:UP000003085};
RN [1] {ECO:0000313|Proteomes:UP000003085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19194 {ECO:0000313|Proteomes:UP000003085};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R., Gibbs R.;
RT "Complete sequence of Mobiluncus curtisii ATCC 43063.";
RL Submitted (MAR-2010) 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:EFF82509.1}.
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DR EMBL; ADMT01000175; EFF82509.1; -; Genomic_DNA.
DR AlphaFoldDB; D4XQM3; -.
DR HOGENOM; CLU_002162_0_1_6; -.
DR Proteomes; UP000003085; 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:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004847; F:urea carboxylase activity; IEA:UniProtKB-EC.
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; IPR001882; Biotin_BS.
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; PS00188; BIOTIN; 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}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EFF82509.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 6..450
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 125..322
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1131..1206
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 1206 AA; 133934 MW; 3999084B9C27C7B8 CRC64;
MGEIIMFKTV LIANRGEIAV RAIRTLKRLG VTSVAVYSDS DRYAQHVEDA DIAIALDGLK
PADTYLSIEK LIQAAKQTGA EAIFPGYGFL SESADFSRAC EENNIAFMGP TAEQILEFGL
KHRARELAAA ANVPMTPGTG LLDSLEEALT AADRIGYPIM LKSTAGGGGI GLTRCDTPQA
LTNAYESVKR LGEQFFKDAG VFIECFIDKA RHVEVQIFGD GKGQVVAFGE RDCSLQRRNQ
KVVEETPAAN LPEATRKKLH QAAIELGKSV NYRSAGTVEF IYDANRDEFY FLEVNTRLQV
EHPVTEMVTG LDLIECMLKV AAGDELDWAY LSNIQPKGAA IEVRVYAEDP VKNFQPSPGV
LTEVAFPEGI RVDTWVKTGT EISQYFDPMI AKIIVHADDR ASAIEKLKNV LAETRLNGIS
TNLDYARAIV SDQRFESMQI WTRMLDDFNY TPNVIEVVQA GTLSSIQDYP GRTGYWDIGV
PPSGPMDDYA FQLANRIAGN DAKAAGFEFT LVGPTLKFHT DTIIALAGAS CIALLDDQEI
DFWTPVEVKA GQILKIGQVE SGCRTYLAVR NGLDVPVYLG SRSTFALGNF GGHAGRTLRV
GDMIKMVDPA FASAELPLAH DEPQALSAEL IPEYSNEWEI AVLYGPHGAP DFFKPEYVEE
FFASEWTVHF NSNRLGVRLS GPTPSWAREN GGEAGLHPSN VHDCEYAIGA INFTGDFPVI
LAKDGPSLGG FVCPVTIAKA ELWKVGQLKA DDKIRFYPIS VEQANELERQ QIENIQNFAE
ASKIVETIEP IQEVVSTILA QREPTELSPK TVYRQAGDSY ILLEYGENVL DLALRLRVHQ
LIQMIRDAKI AGVLELSPGV RSLQIKYDGL IIPQSQLIAH LLQLEEEMGD LSQLKIPSRI
VHLPMAFEDS ATLGAVERYQ ESVCSKAPWL PNNVDFIQRI NGLADRNEVK DIIFDANYLI
LGLGDVYLTA PCAVPIDPRH RLLSSKYNPA RTFTAEGTVG IGGMYMCIYG MDSPGGYQLI
GRTLPIWNKF KKNKQFGDKQ WFLQFFDQIK YFEVTEEELN QWRADFENGY AQIKIEETEF
DYADYVKFLD DEAESIAEFK ARQQQAFTTE VDRWKEEFAA QPEEQIQENN HADYSHLASL
NASMTGNIWK IFVEHGQEVK KGETVAIIEA MKMELPVYAE EDGIVKAIIC RAGQTVHSGE
PLVYME
//