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Database: UniProt
Entry: D1BIG8_SANKS
LinkDB: D1BIG8_SANKS
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ID   D1BIG8_SANKS            Unreviewed;       425 AA.
AC   D1BIG8;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   24-JAN-2024, entry version 82.
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   OrderedLocusNames=Sked_22300 {ECO:0000313|EMBL:ACZ22145.1};
OS   Sanguibacter keddieii (strain ATCC 51767 / DSM 10542 / NCFB 3025 / ST-74).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Sanguibacteraceae;
OC   Sanguibacter.
OX   NCBI_TaxID=446469 {ECO:0000313|EMBL:ACZ22145.1, ECO:0000313|Proteomes:UP000000322};
RN   [1] {ECO:0000313|EMBL:ACZ22145.1, ECO:0000313|Proteomes:UP000000322}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51767 / DSM 10542 / NCFB 3025 / ST-74
RC   {ECO:0000313|Proteomes:UP000000322};
RX   PubMed=21304646;
RA   Ivanova N., Sikorski J., Sims D., Brettin T., Detter J.C., Han C.,
RA   Lapidus A., Copeland A., Glavina Del Rio T., Nolan M., Chen F., Lucas S.,
RA   Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Pati A.,
RA   Mavromatis K., Chen A., Palaniappan K., D'haeseleer P., Chain P.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Goker M., Pukall R.,
RA   Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Sanguibacter keddieii type strain (ST-74).";
RL   Stand. Genomic Sci. 1:110-118(2009).
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}.
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DR   EMBL; CP001819; ACZ22145.1; -; Genomic_DNA.
DR   RefSeq; WP_012867214.1; NC_013521.1.
DR   AlphaFoldDB; D1BIG8; -.
DR   STRING; 446469.Sked_22300; -.
DR   KEGG; ske:Sked_22300; -.
DR   eggNOG; COG4992; Bacteria.
DR   HOGENOM; CLU_016922_10_1_11; -.
DR   OMA; MVPGFKY; -.
DR   OrthoDB; 3246809at2; -.
DR   UniPathway; UPA00068; UER00109.
DR   Proteomes; UP000000322; Chromosome.
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; 3.
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:ACZ22145.1};
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};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01107, ECO:0000313|EMBL:ACZ22145.1}.
FT   BINDING         125..126
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
FT   BINDING         151
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
FT   BINDING         154
FT                   /ligand="N(2)-acetyl-L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:57805"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
FT   BINDING         241..244
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
FT   BINDING         303
FT                   /ligand="N(2)-acetyl-L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:57805"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
FT   BINDING         304
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
FT   MOD_RES         274
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01107"
SQ   SEQUENCE   425 AA;  43832 MW;  4F0EDA6687916B71 CRC64;
     MSALDPRTDT SADLTGPGSG AEWTARYSGA VMDTFGPPQR VLVRGEGAYV WDADGRRYLD
     LLGGIAVNSL GHAHPTLTAA ISAQLGTLGH VSNFFGTPTQ VALAERLLDL SAAPEGSRVF
     FSNSGTEANE AAFKMARRTG RPRILALEGS FHGRSMGALA LTSKAAYREP FEPLPGGVEF
     LPFGDLDALE AAFAGDPATS DVAAVFLEPV QGEAGVRPVS ATYLQRVREL TREHGALMIL
     DEVQTGMGRT GTWLAHHLPQ IGGGIVPDVV TLAKGLGGGF PIGAVVAYGH GPAALLGRGQ
     HGTTFGGNPV AAAAALATIG VIERDGLLTS VRTVGDHLRT RVAGLGHPLV VATRGEGLLV
     AVELSAPVSA VVAARALDAG FIVNPVTPTA LRLAPPLILT REQADDFVAF LAALPTDPAD
     LTTEA
//
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