ARUC_PSEAE
ID ARUC_PSEAE Reviewed; 406 AA.
AC O30508;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Succinylornithine transaminase/acetylornithine aminotransferase;
DE Short=ACOAT;
DE Short=SOAT;
DE Short=Succinylornithine aminotransferase;
DE EC=2.6.1.11;
DE EC=2.6.1.81;
GN Name=aruC; Synonyms=argD, astC; OrderedLocusNames=PA0895;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, INDUCTION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=9393691; DOI=10.1128/jb.179.23.7280-7290.1997;
RA Itoh Y.;
RT "Cloning and characterization of the aru genes encoding enzymes of the
RT catabolic arginine succinyltransferase pathway in Pseudomonas aeruginosa.";
RL J. Bacteriol. 179:7280-7290(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-25.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=9286980; DOI=10.1128/jb.179.17.5300-5308.1997;
RA Park S.-M., Lu C.-D., Abdelal A.T.;
RT "Cloning and characterization of argR, a gene that participates in
RT regulation of arginine biosynthesis and catabolism in Pseudomonas
RT aeruginosa PAO1.";
RL J. Bacteriol. 179:5300-5308(1997).
CC -!- FUNCTION: Transaminates both N(2)-acetylornithine and N(2)-
CC succinylornithine.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + N(2)-succinyl-L-ornithine = L-glutamate + N-
CC succinyl-L-glutamate 5-semialdehyde; Xref=Rhea:RHEA:16953,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:58514,
CC ChEBI:CHEBI:58520; EC=2.6.1.81;
CC Evidence={ECO:0000269|PubMed:9393691};
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;
CC Evidence={ECO:0000269|PubMed:9393691};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.4 mM for N(2)-succinyl-L-ornithine (at 15 mM 2-ketoglutarate and
CC pH 9.0) {ECO:0000269|PubMed:9393691};
CC KM=1.1 mM for N(2)-acetyl-L-ornithine (at pH 9.0)
CC {ECO:0000269|PubMed:9393691};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 4/4.
CC -!- PATHWAY: Amino-acid degradation; L-arginine degradation via AST
CC pathway; L-glutamate and succinate from L-arginine: step 3/5.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Induced by arginine and repressed by succinate.
CC {ECO:0000269|PubMed:9393691}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. ArgD subfamily. {ECO:0000305}.
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DR EMBL; AF011922; AAC46009.1; -; Genomic_DNA.
DR EMBL; AF008308; AAC45654.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG04284.1; -; Genomic_DNA.
DR PIR; H83532; H83532.
DR RefSeq; NP_249586.1; NC_002516.2.
DR RefSeq; WP_003112608.1; NZ_QZGE01000007.1.
DR AlphaFoldDB; O30508; -.
DR SMR; O30508; -.
DR STRING; 287.DR97_1048; -.
DR PaxDb; O30508; -.
DR PRIDE; O30508; -.
DR EnsemblBacteria; AAG04284; AAG04284; PA0895.
DR GeneID; 878207; -.
DR KEGG; pae:PA0895; -.
DR PATRIC; fig|208964.12.peg.930; -.
DR PseudoCAP; PA0895; -.
DR HOGENOM; CLU_016922_10_1_6; -.
DR InParanoid; O30508; -.
DR OMA; MVPNYNP; -.
DR PhylomeDB; O30508; -.
DR BioCyc; MetaCyc:MON-11526; -.
DR BioCyc; PAER208964:G1FZ6-911-MON; -.
DR BRENDA; 2.6.1.81; 5087.
DR UniPathway; UPA00068; UER00109.
DR UniPathway; UPA00185; UER00281.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR GO; GO:0003992; F:N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity; IDA:PseudoCAP.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0043825; F:succinylornithine transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0006526; P:arginine biosynthetic process; IDA:PseudoCAP.
DR GO; GO:0006527; P:arginine catabolic process; IDA:PseudoCAP.
DR GO; GO:0019545; P:arginine catabolic process to succinate; IEA:UniProtKB-UniPathway.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_01107; ArgD_aminotrans_3; 1.
DR InterPro; IPR017652; Ac/SucOrn_transaminase_bac.
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 Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR03246; arg_catab_astC; 1.
DR TIGRFAMs; TIGR00707; argD; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Aminotransferase; Arginine biosynthesis;
KW Arginine metabolism; Cytoplasm; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..406
FT /note="Succinylornithine transaminase/acetylornithine
FT aminotransferase"
FT /id="PRO_0000112768"
FT BINDING 108..109
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="N(2)-acetyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:57805"
FT /evidence="ECO:0000250"
FT BINDING 226..229
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="N(2)-acetyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:57805"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT MOD_RES 255
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 406 AA; 43748 MW; 6758B41248F751AB CRC64;
MSAPHAQVER ADFDRYMVPN YAPAAFIPVR GEGSRVWDQS GRELIDFAGG IAVTSLGHAH
PALVKALTEQ AQRIWHVSNV FTNEPALRLA RKLVDATFAE RVFLANSGAE ANEAAFKLAR
RYANDVYGPQ KYEIIAASNS FHGRTLFTVN VGGQPKYSDG FGPKFEGITH VPYNDLEALK
AAISDKTCAV VLEPIQGEGG VLPAQQAYLE GARKLCDEHN ALLVFDEVQS GMGRVGELFA
YMHYGVVPDI LSSAKSLGGG FPIGAMLTTG EIAKHLSVGT HGTTYGGNPL ASAVAEAALD
VINTPEVLDG VKAKHERFKS RLQKIGQEYG IFDEIRGMGL LIGAALTDEW KGKARDVLNA
AEKEAVMVLQ ASPDVVRFAP SLVIDDAEID EGLERFERAV AKLVRG
