ID A0A2I0MR36_COLLI Unreviewed; 1179 AA.
AC A0A2I0MR36;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Mycocerosic acid synthase-like {ECO:0000313|EMBL:PKK32149.1};
GN ORFNames=A306_00002491 {ECO:0000313|EMBL:PKK32149.1};
OS Columba livia (Rock dove).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX NCBI_TaxID=8932 {ECO:0000313|EMBL:PKK32149.1, ECO:0000313|Proteomes:UP000053872};
RN [1] {ECO:0000313|EMBL:PKK32149.1, ECO:0000313|Proteomes:UP000053872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Blood {ECO:0000313|EMBL:PKK32149.1};
RX PubMed=23371554; DOI=10.1126/science.1230422;
RA Shapiro M.D., Kronenberg Z., Li C., Domyan E.T., Pan H., Campbell M.,
RA Tan H., Huff C.D., Hu H., Vickrey A.I., Nielsen S.C., Stringham S.A.,
RA Hu H., Willerslev E., Gilbert M.T., Yandell M., Zhang G., Wang J.;
RT "Genomic diversity and evolution of the head crest in the rock pigeon.";
RL Science 339:1063-1067(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP];
CC Xref=Rhea:RHEA:41792, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449; EC=2.3.1.39;
CC Evidence={ECO:0000256|ARBA:ARBA00023404};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41793;
CC Evidence={ECO:0000256|ARBA:ARBA00023404};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005194}.
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:PKK32149.1}.
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DR EMBL; AKCR02000004; PKK32149.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0MR36; -.
DR STRING; 8932.A0A2I0MR36; -.
DR InParanoid; A0A2I0MR36; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000053872; Unassembled WGS sequence.
DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR PANTHER; PTHR45681:SF6; CARRIER DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45681; POLYKETIDE SYNTHASE 44-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000053872};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 20..318
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
FT DOMAIN 382..540
FT /note="Polyketide synthase dehydratase"
FT /evidence="ECO:0000259|SMART:SM00826"
SQ SEQUENCE 1179 AA; 131640 MW; C5DC6731247DCD25 CRC64;
MSAASTELAT SKAEPQLVFV FCGNGVTLKD FSEVLLSSEP VFRDKCKEIE ALFQKHAPIS
LLPARGHSPK DLLNPELSQP LLFTLQVALA ALLKYWGIKP VAVVGHSVGE VAAAHFAGYL
SLADAVKVIY HRSRLQAKTA GGRMLVVGNI PVQELAEHLH RYSGKVCIAA FNSPVSCTLS
GNSDSVDAVQ RDLAQVFSQR NIFLHVLNVP AAYHSPSMDM ILGELEDNIQ PLEKQKGEIE
VISTLTGVAA SENDFSQGKF WARHAREPVA FSQAIKTAAR DRENVVFVEI SPHRALQRSI
METLGKGTKV FSSLQTDAEY QTLFTLVGDL FELGYNPNWQ HFYNGYQSVP VAIPRYQFDR
KKLMACLDIH QQANQRGVSC SHPLIYDINS DNTEYGCLLS QDTTSYLYEH KNNGVALVPG
AFYVELGLAS VMSSSRPRVP LSACRMSISF SAPCVLTESS QVLRIKLSPQ KAVTAFEILS
SSNAVYAAGQ VTKGPEAVVE ESSISCQDIY RRCRSVVSRE AVYEALSHVG FQYGSIFRQL
SDVHYCQELK EAITSIKVNK ETIKEMYSYH IHPVLLDCFL QMTAFMTART CQSRAGFPSG
IGSMVVLRPL EEEMMIYMRT SKSIGNYLEV CGCFTDKCGS VLAELKRVAI IFTKQESSRE
NEFMFENKWK EVSLSQMIGH LGSMPRVLVF ADRFGIAEQL KKYLHPDSRY VMYEDWEALL
GGHAQNKMRA DVEDYDEILF LWGIQKLNED FPSKVVDQLA KCCEAYRQVI VALREKASRC
LVRVITYRTT ERHVDHINCG FALCGMTRTC VVEVPDVTFQ MIDLSSSSSL DISVLADVLV
KYKVVDYPEV CISQGRTYVA EIRRTPFVDS DHSQPVRSLQ KSETFTLHTS DPYTAKDLSA
ELSTSPATQL DKWSVEIQLD KICLHSEDYF PISVSSHNFG NTLYWNSQAV DKHRLLALDF
SGTVTATGTD VKKVKVGDHV VSCYPAAASS RLRIPGTACF NVKKFPCFQN VPCMSYFIIA
WEILNQKLPK GRHGRTLGII STEPSSVLCH VLSAAAEEMG WRTALARPTP DGFQYIKSCS
ALVVLPPVSR LSQEDLAHMY FLKDVVIVCG SRQSECIQNV SDIDHENISF HILTLTSIFQ
KASLKELQKT VHVWIRSMDM KRFRHLSGSV FSGLRTLKE
//
