ID   A0A143HMR6_9GAMM        Unreviewed;      1209 AA.
AC   A0A143HMR6;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Urea carboxylase {ECO:0000313|EMBL:AMX02821.1};
GN   ORFNames=A3224_09720 {ECO:0000313|EMBL:AMX02821.1};
OS   Microbulbifer thermotolerans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Microbulbiferaceae; Microbulbifer.
OX   NCBI_TaxID=252514 {ECO:0000313|EMBL:AMX02821.1, ECO:0000313|Proteomes:UP000076077};
RN   [1] {ECO:0000313|Proteomes:UP000076077}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAU221 {ECO:0000313|Proteomes:UP000076077};
RA   Lee Y.-S., Choi Y.-L.;
RL   Submitted (MAR-2016) 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; CP014864; AMX02821.1; -; Genomic_DNA.
DR   RefSeq; WP_067153849.1; NZ_CP014864.1.
DR   AlphaFoldDB; A0A143HMR6; -.
DR   STRING; 252514.A3224_09720; -.
DR   GeneID; 76608328; -.
DR   KEGG; mthd:A3224_09720; -.
DR   OrthoDB; 9763189at2; -.
DR   Proteomes; UP000076077; Chromosome.
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:UP000076077}.
FT   DOMAIN          1..448
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          1119..1197
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   1209 AA;  132945 MW;  FC81A6402B46E202 CRC64;
     MFTKVLIANR GAIATRVIRT LRRMGIASVA VYAECDADSL HVRHADEAYS LGEGAAADTY
     LNVERLLEIA ADSGAQAIHP GYGFLSENAA FVGRCEAAGI TFIGPTAEQM QAFGLKHRAR
     ALAEAAGVPL LPGSELLTDL AAARAEAQRI GYPVMLKSTA GGGGIGMQLC HDVAELDAAF
     DSVKRLGANN FADDGVFLEK FIARARHIEV QVVGDGSGRA LAIGERDCSS QRRNQKVVEE
     CPAPNLSEAV RTRLHSTAEK LLASVEYRNA GTVEFIYDAD SGDFYFLEVN TRLQVEHGVT
     EEVYGVDLVE WMLRIAAGEA PDLEAQRAQL KPTGHAIQVR LYAEDPWRDF QPCAGLLSHV
     SFPEGEGVRI DHWIESGIEV PPFFDPMLAK VIVRAGDRPA ALEKLQQTLD ATELYGSETN
     LDYLRALSRD DTLARGQVTT RYLNSFRYQP ARIDVLQGGT QTTIQDFPGR QGHWDVGVPP
     SGPFDSRSFR LANRLLGNPD SAAGLEITLQ GPTLTFACDT RIALTGATID ATLDGQAIPG
     WQIVPVAAGQ ILQLGRVRAG ARAYLAVCGG IQCPGYLNSR STFTLGQFGG HNGRALRTGD
     VLHLDAAADP GSVSVRGGAE ALRPVLDHHW ELRVIYGPHG APDFFTDEDM RTFFDTDWEI
     HYNSSRTGVR LIGPKPQWAR RDGGEAGLHP SNIHDNAYAF GTVDFTGDMP VILGPDGPSL
     GGFVCPATVI TADLWKLGQL RAGDKVRFVP VSLEQAVALE AAQNRAIETL QAQTCSWQPV
     EPDTPILARF DAETFGDEIV CRAAGDHFLL VEYGPQALDI RLRFRAHALM QWLQQHPLPG
     LRELTPGIRS LQIHFDTQEL SHKHLLAHIE KGERELSQQL AQLSVPSRIV HLPLSWDDAA
     CRLAIEKYEQ SVRRNAPWCP SNLEFIRRIN GLDSIDQVKQ IVFNASYMVM GLGDVYLGAP
     VATPVDPRHR LVTTKYNPAR TWTAENSVGI GGSYLCVYGM EGPGGYQFVG RTLQMWNRYR
     RTDAFEKPWL LRFFDQIRFY EVSHEELQQI RRDFPQGRYP LKIEDSHFSL AEYEQFVADN
     AGDIQTFLEQ RNEAFQEELE RWHANGQFNF EVEEAEAESI EQSWPEDATL VDSPVSGSVW
     QTEVRAGDTV EAGQLLMILE SMKMEIPICA PCSGVVSQLL SNQGGRVSAG QALVVLEDEA
     TLTTGEDKV
//