ID B3RIZ4_TRIAD Unreviewed; 703 AA.
AC B3RIZ4;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial {ECO:0008006|Google:ProtNLM};
GN ORFNames=TRIADDRAFT_18834 {ECO:0000313|EMBL:EDV29275.1};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV29275.1, ECO:0000313|Proteomes:UP000009022};
RN [1] {ECO:0000313|EMBL:EDV29275.1, ECO:0000313|Proteomes:UP000009022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV29275.1,
RC ECO:0000313|Proteomes:UP000009022};
RX PubMed=18719581; DOI=10.1038/nature07191;
RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA Rokhsar D.S.;
RT "The Trichoplax genome and the nature of placozoans.";
RL Nature 454:955-960(2008).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; DS985241; EDV29275.1; -; Genomic_DNA.
DR RefSeq; XP_002108477.1; XM_002108441.1.
DR AlphaFoldDB; B3RIZ4; -.
DR STRING; 10228.B3RIZ4; -.
DR EnsemblMetazoa; TriadT18834; TriadP18834; TriadG18834.
DR GeneID; 6748894; -.
DR KEGG; tad:TRIADDRAFT_18834; -.
DR CTD; 6748894; -.
DR eggNOG; KOG0238; Eukaryota.
DR HOGENOM; CLU_000395_3_1_1; -.
DR InParanoid; B3RIZ4; -.
DR OMA; FINKPKH; -.
DR OrthoDB; 1129179at2759; -.
DR PhylomeDB; B3RIZ4; -.
DR Proteomes; UP000009022; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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; 3.30.700.40; -; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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:UP000009022}.
FT DOMAIN 24..470
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 143..340
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 621..697
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 703 AA; 77905 MW; 7A4C2703595415D4 CRC64;
MIRLFYFIIH QNHLFIPIEV KRKKISKVLI ANRGEIACRV IKTAKSMGIK TVAVYSSADQ
GSMHVEMADE AYYIGEAPSR DSYLRGDKIL DIANYCGAQA IHPGYGFLSE NADFAELCES
QGIVFIGPPA SAIRDMGLKS TSKQIMADAG VPIIEGYHGE DQADAKLKDE ASRIGYPVML
KAVCGGGGKG MRIVMNEGEF DQALESARRE SLKSFNDDKM IVEKYIEEPR HVEVQVFADQ
HGNAVYLSER DCSVQRRHQK IIEEAPAPGL SESIRHEIGA AAVRAAKAVN YVGAGTVEFI
MDKHKKFFFM EMNTRLQVEH PVTELVTNTD LVEWQLQVAS GKELPLLQGD IEPYGHAAEA
RIYAEDPNNN FLPGAGPLRH LKFPLNSDSV RIDTGVTQGD NVSVHYDPMI AKLIVWGEDR
ESALRKLVYS LNECHVVGLN TNLRFLTDLA SHPEFIAGNV HTGFIQEHEN SLFESTKSVL
SCDQSALACL SLLLFEQKDG LLRDMFISQD LYSPWNSTSG LRFNTLYSKS VTLMDGESEM
NFLVTYNRDG SYSIKLSDTL EMEVAGKIFD AEDDDTIFIN AVVNGVKHTA SVVRYNDCLH
IFTADDSFKV QVPLPKFVTM QQDSAITGAG TVAPMTGAII KVLVENGQKV EAGDVLMLIE
AMKMEHKIVS PRSATVKTVL FQEGDSVEKD QSLIIFEESE DNE
//
