ID   G1KR54_ANOCA            Unreviewed;       418 AA.
AC   G1KR54;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=Glycine C-acetyltransferase {ECO:0000313|Ensembl:ENSACAP00000015214.2};
GN   Name=GCAT {ECO:0000313|Ensembl:ENSACAP00000015214.2};
OS   Anolis carolinensis (Green anole) (American chameleon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Iguania; Dactyloidae; Anolis.
OX   NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000015214.2, ECO:0000313|Proteomes:UP000001646};
RN   [1] {ECO:0000313|Ensembl:ENSACAP00000015214.2, ECO:0000313|Proteomes:UP000001646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000015214.2,
RC   ECO:0000313|Proteomes:UP000001646};
RG   The Genome Sequencing Platform;
RA   Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA   Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSACAP00000015214.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008392}.
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DR   RefSeq; XP_003221017.1; XM_003220969.3.
DR   AlphaFoldDB; G1KR54; -.
DR   STRING; 28377.ENSACAP00000015214; -.
DR   Ensembl; ENSACAT00000015522.4; ENSACAP00000015214.2; ENSACAG00000015453.4.
DR   GeneID; 100562818; -.
DR   KEGG; acs:100562818; -.
DR   CTD; 23464; -.
DR   eggNOG; KOG1359; Eukaryota.
DR   GeneTree; ENSGT00940000155729; -.
DR   HOGENOM; CLU_015846_11_0_1; -.
DR   InParanoid; G1KR54; -.
DR   OMA; GTHEYCD; -.
DR   OrthoDB; 9643at2759; -.
DR   TreeFam; TF105923; -.
DR   Proteomes; UP000001646; Chromosome 5.
DR   Bgee; ENSACAG00000015453; Expressed in kidney and 12 other cell types or tissues.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR   GO; GO:0008890; F:glycine C-acetyltransferase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0006567; P:threonine catabolic process; IEA:InterPro.
DR   CDD; cd06454; KBL_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   HAMAP; MF_00985; 2am3keto_CoA_ligase; 1.
DR   InterPro; IPR011282; 2am3keto_CoA_ligase.
DR   InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR01822; 2am3keto_CoA; 1.
DR   PANTHER; PTHR13693:SF102; 2-AMINO-3-KETOBUTYRATE COENZYME A LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR13693; CLASS II AMINOTRANSFERASE/8-AMINO-7-OXONONANOATE SYNTHASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001646};
KW   Transferase {ECO:0000256|ARBA:ARBA00023315}.
FT   DOMAIN          65..407
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   418 AA;  45214 MW;  C20088C72ABC8EF4 CRC64;
     MWARSGLFFG ASRPLGARLR SALAQLEHVL EGELEGIRGA GTWKSERVIL SKQGPHIQVE
     GSRGDILNFC ANNYLGLSSH PEVIRSGLDA LKQYGAGLSS VRFICGTQNI HKDLEEKIAL
     FHQREDAILY ASCFDANAGL FEALLTPEDA VVSDELNHAS IIDGIRLCKA NKYRYKHMDM
     QDLEAKLQDA QKCRLRMVVT DGAFSMDGDI APLKEICSLA QKYNAIVFID ECHATGFLGP
     NGRGTDELLG VMDKVTIINS TLGKALGGAA GGYTTGPKAL VDLLRQRSRP YLFSNSLPPA
     VVGCASKALD LLMKSNAIAQ SMAAKTTRFR SKMAAAGFTI SGSDHPICPV MLGDARLASG
     MADDMLKRGI YVIGFSYPVV PKGKARIRVQ ISAVHSEEDI DRCVEAFTEV GRKHGALP
//