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
//