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Database: UniProt
Entry: A0A222E674_9RHOB
LinkDB: A0A222E674_9RHOB
Original site: A0A222E674_9RHOB 
ID   A0A222E674_9RHOB        Unreviewed;       646 AA.
AC   A0A222E674;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Acetyl-/propionyl-coenzyme A carboxylase alpha chain {ECO:0000313|EMBL:ASP21719.1};
GN   ORFNames=ANTHELSMS3_03067 {ECO:0000313|EMBL:ASP21719.1};
OS   Antarctobacter heliothermus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Antarctobacter.
OX   NCBI_TaxID=74033 {ECO:0000313|EMBL:ASP21719.1, ECO:0000313|Proteomes:UP000203589};
RN   [1] {ECO:0000313|EMBL:ASP21719.1, ECO:0000313|Proteomes:UP000203589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMS3 {ECO:0000313|EMBL:ASP21719.1,
RC   ECO:0000313|Proteomes:UP000203589};
RA   Topel M., Pinder M.I.M., Johansson O.N., Kourtchenko O., Godhe A.,
RA   Clarke A.K.;
RT   "Genome Sequence of Antarctobacter heliothermus Strain SMS3 Isolated from a
RT   culture of the Diatom Skeletonema marinoi.";
RL   Submitted (JUL-2017) 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; CP022540; ASP21719.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A222E674; -.
DR   KEGG; aht:ANTHELSMS3_03067; -.
DR   OrthoDB; 9763189at2; -.
DR   Proteomes; UP000203589; Chromosome.
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; 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:UP000203589}.
FT   DOMAIN          1..448
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          120..321
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          566..641
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   646 AA;  68242 MW;  3A373C25F1780FF3 CRC64;
     MFDTILIANR GEIAARVIRT ARSMGLRCVA VHSDVDADAL HVELADEAVC IGGAAPSQSY
     LRGDVIIEAA KATGAQAIHP GYGFLSENPD FVQAVEAAGL TFIGPSAQAI RQMGLKDSAK
     RLMQAAGVPV VPGYMGEDQD PGHLEVEALK VGYPLLIKAV AGGGGKGMRL VERPEDFVDA
     LERAKAEART AFGNDAVLIE KFIQRPRHIE VQVFGDGNRA VHLFERDCSL QRRHQKVIEE
     APAPGMTAEM RAAMGQAAVK AAEAIAYKGA GTVEFIVDGA NGLRPDGFWF MEMNTRLQVE
     HPVTEEICGV DLVEWQIRVA AGEPLPAVQD DLTINGHAFE ARLYAEDVPA GFLPATGTLA
     ELAFPEGVRA EAGVRSGDAI SPHYDPMIAK LVVHGPSRAV ALRRLARGLR DTRVAGTVTN
     LGFLGALAEH EGFARGEVDT GLIGRDLDAL MAPAEVTPQI WAEAAMAALG LLETQGWDAG
     FTLWGAEWRA VVLEQGGETR EIGVKLHGPD AALVRVVGQE VTAARGVRGW TFDGKPGAGS
     HVTRGHVTVY ADYGVGFARP DPLARGVGVQ AAAGALAPMP GRVVSVHVAV GQAVEEGDRL
     VVLEAMKMEH TLRAGRAGQV AEVLVAEGDQ VEAGAPLVVL VEEDEA
//
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