ID A0A0Q5VH32_9ACTN Unreviewed; 543 AA.
AC A0A0Q5VH32;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Acetyl-CoA carboxylase carboxyltransferase subunit {ECO:0000313|EMBL:KQS60838.1};
GN ORFNames=ASG36_08250 {ECO:0000313|EMBL:KQS60838.1};
OS Geodermatophilus sp. Leaf369.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=1736354 {ECO:0000313|EMBL:KQS60838.1, ECO:0000313|Proteomes:UP000051830};
RN [1] {ECO:0000313|EMBL:KQS60838.1, ECO:0000313|Proteomes:UP000051830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf369 {ECO:0000313|EMBL:KQS60838.1,
RC ECO:0000313|Proteomes:UP000051830};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQS60838.1, ECO:0000313|Proteomes:UP000051830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf369 {ECO:0000313|EMBL:KQS60838.1,
RC ECO:0000313|Proteomes:UP000051830};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQS60838.1}.
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DR EMBL; LMQA01000001; KQS60838.1; -; Genomic_DNA.
DR RefSeq; WP_055761773.1; NZ_LMQA01000001.1.
DR AlphaFoldDB; A0A0Q5VH32; -.
DR STRING; 1736354.ASG36_08250; -.
DR OrthoDB; 9803706at2; -.
DR Proteomes; UP000051830; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR InterPro; IPR034733; AcCoA_carboxyl_beta.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR011762; COA_CT_N.
DR InterPro; IPR045190; MCCB/AccD1-like.
DR PANTHER; PTHR22855; ACETYL, PROPIONYL, PYRUVATE, AND GLUTACONYL CARBOXYLASE-RELATED; 1.
DR PANTHER; PTHR22855:SF46; METHYLCROTONOYL-COA CARBOXYLASE; 1.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 2.
DR PROSITE; PS50989; COA_CT_CTER; 2.
DR PROSITE; PS50980; COA_CT_NTER; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000051830};
KW Transferase {ECO:0000313|EMBL:KQS60838.1}.
FT DOMAIN 33..284
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 39..276
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT DOMAIN 284..534
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 543 AA; 57942 MW; 803DA123B04C2A89 CRC64;
MTVSADPRVT EGTVLTSLLD TRGDQYRTNR TASLAVLDQL EEQLDLVRAG GGERYQARHR
DRGRLLARER IELLLDRDAA FLELSSLAAW GTPFTVGASI VTGIGVVSGV ECVLIAHDPT
VRGGAMNPIS LKKTLRALEI ARRNRLPVVN LVESGGADLP SQADLFVNAG QIFHDLTELS
SMGVPTIALV FGNSTAGGAY VPGMCDYSVL VDQQAKVFLG GPPLVKMATG EDADDEELGG
AAMHARVSGV ADHFAVDERD AIRLGRRIIS ELNWRKQGPG PSLPADEPLF DPEELLGIAP
ADIRVPFDPR EVLARVVDGS RFGEYKPEYG TSLVTGFASV HGFPVGVLAN ARGVLFSEEA
KKAAEFIQLA NQVDTPLVFL QNTTGYMVGK SYEQGGIIKD GAKMINAVTN STVPHITINT
AASFGAGNYG MSGRAYDPRL MFAWAGAKLA VMGATQLAGV MSIVGKASAE ASGRPFDQAA
DDERRRGIEA QIEAESHSFF VTSKVYDDGL LDPRDTRTVL GIALSAAHSG PIEGRRGYGV
FRM
//
