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
//