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Database: UniProt
Entry: H5T9D1_9ALTE
LinkDB: H5T9D1_9ALTE
Original site: H5T9D1_9ALTE 
ID   H5T9D1_9ALTE            Unreviewed;       680 AA.
AC   H5T9D1;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial {ECO:0000313|EMBL:GAB54908.1};
GN   Name=mccA {ECO:0000313|EMBL:GAB54908.1};
GN   ORFNames=GPUN_0770 {ECO:0000313|EMBL:GAB54908.1};
OS   Glaciecola punicea ACAM 611.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Glaciecola.
OX   NCBI_TaxID=1121923 {ECO:0000313|EMBL:GAB54908.1, ECO:0000313|Proteomes:UP000053586};
RN   [1] {ECO:0000313|EMBL:GAB54908.1, ECO:0000313|Proteomes:UP000053586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACAM 611 {ECO:0000313|EMBL:GAB54908.1,
RC   ECO:0000313|Proteomes:UP000053586};
RX   PubMed=22628500; DOI=10.1128/JB.00463-12;
RA   Qin Q.-L., Xie B.-B., Shu Y.-L., Rong J.-C., Zhao D.-L., Zhang X.-Y.,
RA   Chen X.-L., Zhou B.-C., Zhanga Y.-Z.;
RT   "Genome sequence of proteorhodopsin-containing sea ice bacterium Glaciecola
RT   punicea ACAM 611T.";
RL   J. Bacteriol. 194:3267-3267(2012).
RN   [2] {ECO:0000313|EMBL:GAB54908.1, ECO:0000313|Proteomes:UP000053586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACAM 611 {ECO:0000313|EMBL:GAB54908.1,
RC   ECO:0000313|Proteomes:UP000053586};
RX   PubMed=25009843;
RA   Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA   Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT   "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT   high degree of genomic diversity and genomic characteristic for cold
RT   adaptation.";
RL   Environ. Microbiol. 16:1642-1653(2014).
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:GAB54908.1}.
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DR   EMBL; BAET01000007; GAB54908.1; -; Genomic_DNA.
DR   RefSeq; WP_006003474.1; NZ_BAET01000007.1.
DR   AlphaFoldDB; H5T9D1; -.
DR   STRING; 56804.BAE46_00215; -.
DR   eggNOG; COG4770; Bacteria.
DR   OrthoDB; 9763189at2; -.
DR   Proteomes; UP000053586; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; 3.30.470.20; ATP-grasp fold, B domain; 1.
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; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
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   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding 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   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000053586}.
FT   DOMAIN          1..447
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          588..664
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   680 AA;  74553 MW;  C70B66D33C16C6B2 CRC64;
     MIKKILIANR GEIACRVMKS AHKLGIATVA VYSQADTNAQ HVKMANEAVY LGEAPATKSY
     LNGDLIIQKA KSLGVDAIHP GYGFLSENAN FADKCEQNGI IFIGPNSSAI RAMGSKSAAK
     TIMEAANVPL VPGYHGDNQD PSFLRDQANA MGYPVLLKAA AGGGGKGMRQ VWQEKDFFEA
     LDAAKREAMN GFGDDIMLVE KYLTEPRHVE IQVFCDNFGK GVYLFERDCS VQRRHQKIIE
     EAPAPGMTGD IRQQMGEAAL KAAHAIGYTN AGTVEFLLDS DGAFYFMEMN TRLQVEHPVT
     EFITGEDLVE WQIAVANNLP LPKSQDALSI KGHAFEARIY AEDPHNEFLP STGLIEYLLE
     PPKNEHVRID SGVVSGDEVS IYYDPMIAKL VVWAENRDQA LALLITSLQQ YMICGVTTNI
     PYLIQVASSE PFRKAILTTD FIERHGNVIA TNNKKIPDSV QGLSPVQIIA VSAMLSLSNT
     NDVNHNAYTG SVSYPGFRLN HTLAQELEFA HGDNYHRYSQ KHIDKNTWSI TINDIDHVYS
     ASKTQNVLNV DAREHIASYP IYENDDVAWL LDNTGELKVI KPKINMGTEG EKLHAGDVLA
     PMNGTLVAMN VKQGQRVEKD DLLAVVEAMK MEHSMRAPFA GTVSECFGNK GDLVDGGQVL
     VSLKADLADS SAADEQEMSV
//
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