ID B4DHW5_HUMAN Unreviewed; 474 AA.
AC B4DHW5;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=cDNA FLJ53328, highly similar to Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial {ECO:0000313|EMBL:BAG58277.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG58277.1};
RN [1] {ECO:0000313|EMBL:BAG58277.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Caudate nucleus {ECO:0000313|EMBL:BAG58277.1};
RA Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A.,
RA Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y.,
RA Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.,
RA Sugano S., Nomura N., Isogai T.;
RT "NEDO human cDNA sequencing project focused on splicing variants.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; AK295293; BAG58277.1; -; mRNA.
DR AlphaFoldDB; B4DHW5; -.
DR MaxQB; B4DHW5; -.
DR PeptideAtlas; B4DHW5; -.
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 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; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_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; 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 PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 2: Evidence at transcript level;
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 Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
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"
SQ SEQUENCE 474 AA; 52653 MW; 2911DBB0A19B8727 CRC64;
MAAASAVSVL LVAAERNRWH RLPSLLLPPR TWVWRQRTMK YTTATDEAYS IGPAPSQQSY
LSMEKIIQVA KTSAAQAIHP GCGFLSEHME FAELCKQEGI IFIGPPPSAI RDMGIKSTSK
SIMAAAGVPV VEGYHGEDQS DQCLKEHARR IGYPVMIKAV RGGGGKGMRI VRSEQEFQEQ
LESARREAKK SFNDDAMLIE KFVDTPRHIE VQVFGDHHGN AVYLFERDCS VQRRHQKIIE
EAPAPGIKSE VRKKLGEAAV RAAKAVNYVG AGTVEFIMDS KHNFCFMEMN TRLQVEHPVT
EMITGTDLVE WQLRIAAGEK IPLSQEEITL QGHAFEARIY AEDPSNNFMP VAGPLVHLST
PRADPSTRIE TGVRQGDEVS VHYDPMIAKL VVWAADRQAA LTKLRYSLRQ YNIVGLPTNM
TSYSTCLATQ SLKLGTCTLI SSLNTTNSCC SVGRLQPKSL YARQPWVSSS RRKP
//
