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Database: UniProt
Entry: R5R2Y9_9FIRM
LinkDB: R5R2Y9_9FIRM
Original site: R5R2Y9_9FIRM 
ID   R5R2Y9_9FIRM            Unreviewed;       396 AA.
AC   R5R2Y9;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Acetylornithine aminotransferase {ECO:0000256|HAMAP-Rule:MF_01107};
DE            Short=ACOAT {ECO:0000256|HAMAP-Rule:MF_01107};
DE            EC=2.6.1.11 {ECO:0000256|HAMAP-Rule:MF_01107};
GN   Name=argD {ECO:0000256|HAMAP-Rule:MF_01107};
GN   ORFNames=BN747_01863 {ECO:0000313|EMBL:CCZ33084.1};
OS   Firmicutes bacterium CAG:646.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1262995 {ECO:0000313|EMBL:CCZ33084.1, ECO:0000313|Proteomes:UP000018386};
RN   [1] {ECO:0000313|EMBL:CCZ33084.1, ECO:0000313|Proteomes:UP000018386}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:646 {ECO:0000313|Proteomes:UP000018386};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + N(2)-acetyl-L-ornithine = L-glutamate + N-
CC         acetyl-L-glutamate 5-semialdehyde; Xref=Rhea:RHEA:18049,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:29123, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:57805; EC=2.6.1.11; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01107};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01107};
CC       Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01107};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC       L-ornithine from L-glutamate: step 4/4. {ECO:0000256|HAMAP-
CC       Rule:MF_01107}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01107}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01107}.
CC   -!- MISCELLANEOUS: May also have succinyldiaminopimelate aminotransferase
CC       activity, thus carrying out the corresponding step in lysine
CC       biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01107}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. ArgD subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_01107}.
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:CCZ33084.1}.
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DR   EMBL; CAZW010000047; CCZ33084.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5R2Y9; -.
DR   STRING; 1262995.BN747_01863; -.
DR   UniPathway; UPA00068; UER00109.
DR   Proteomes; UP000018386; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003992; F:N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00610; OAT_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_01107; ArgD_aminotrans_3; 1.
DR   InterPro; IPR004636; AcOrn/SuccOrn_fam.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR00707; argD; 1.
DR   PANTHER; PTHR11986:SF79; ACETYLORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_01107};
KW   Aminotransferase {ECO:0000256|HAMAP-Rule:MF_01107,
KW   ECO:0000313|EMBL:CCZ33084.1};
KW   Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01107};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01107};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_01107}; Reference proteome {ECO:0000313|Proteomes:UP000018386};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01107, ECO:0000313|EMBL:CCZ33084.1}.
FT   BINDING         106..107
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
FT   BINDING         139
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
FT   BINDING         142
FT                   /ligand="N(2)-acetyl-L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:57805"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
FT   BINDING         224..227
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
FT   BINDING         282
FT                   /ligand="N(2)-acetyl-L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:57805"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
FT   BINDING         283
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
FT   MOD_RES         253
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
SQ   SEQUENCE   396 AA;  43562 MW;  72BB202F5A181ED5 CRC64;
     MMCSKEYIDR AEQAVLHTYN RFPVVLEKGQ GVRLYDVEGK EYLDFAAGIA VFSLGYNHPE
     YSKTLKEQID KLLHTSNLYY NVPMVEAAEK LTKAAGLSKV FFTNSGTEAV EGAIKVARKY
     AYLKDGSTDH EIIAMNHSFH GRSLGALSVT GNTHYQEPFK PLIGGIRFAD FNDLESVKAQ
     INEKTCAIIM ETVQGEGGIY PATEEFLQGV RKLCDEKDML LILDEIQCGM GRTGSMFACQ
     SYGVQPDVMT CAKALGCGVP VGAFVLNEKT ANASLVPGDH GTTYGGNPFA CAAVSKVFDL
     FEQEHILEHV QQITPYLEEK LDELVDKYPM IMARRGKGLM QGLVLEGKPV GEVVSRALEQ
     GLIVISAGEN VLRLVPPLVI TEEDIDEMVE KLEKSL
//
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