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Multifunctional fusion protein [Includes: Acetylornithine aminotransferase (ACOAT) (EC 2.6.1.11); Ornithine aminotransferase (OAT) (EC 2.6.1.13) (Ornithine--oxo-acid aminotransferase)]

 A0A0A3JTB1_9BACI        Unreviewed;       398 AA.
A0A0A3JTB1;
04-FEB-2015, integrated into UniProtKB/TrEMBL.
04-FEB-2015, sequence version 1.
25-OCT-2017, entry version 22.
RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_01107, ECO:0000256|HAMAP-Rule:MF_01689};
Includes:
RecName: Full=Acetylornithine aminotransferase {ECO:0000256|HAMAP-Rule:MF_01107};
Short=ACOAT {ECO:0000256|HAMAP-Rule:MF_01107};
EC=2.6.1.11 {ECO:0000256|HAMAP-Rule:MF_01107};
Includes:
RecName: Full=Ornithine aminotransferase {ECO:0000256|HAMAP-Rule:MF_01689};
Short=OAT {ECO:0000256|HAMAP-Rule:MF_01689};
EC=2.6.1.13 {ECO:0000256|HAMAP-Rule:MF_01689};
AltName: Full=Ornithine--oxo-acid aminotransferase {ECO:0000256|HAMAP-Rule:MF_01689};
Name=rocD {ECO:0000256|HAMAP-Rule:MF_01689,
ECO:0000313|EMBL:KGR90247.1};
Synonyms=argD {ECO:0000256|HAMAP-Rule:MF_01107};
ORFNames=CD30_12840 {ECO:0000313|EMBL:KGR90247.1};
Lysinibacillus massiliensis 4400831 = CIP 108448 = CCUG 49529.
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae;
Lysinibacillus.
NCBI_TaxID=1211035 {ECO:0000313|EMBL:KGR90247.1, ECO:0000313|Proteomes:UP000030595};
[1] {ECO:0000313|EMBL:KGR90247.1, ECO:0000313|Proteomes:UP000030595}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CCUG 49529 {ECO:0000313|EMBL:KGR90247.1,
ECO:0000313|Proteomes:UP000030595};
Zhang F., Wang G., Zhang L.;
"Draft genome sequence of Lysinibacillus massiliensis CCUG 49529.";
Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the interconversion of ornithine to glutamate
semialdehyde. {ECO:0000256|HAMAP-Rule:MF_01689}.
-!- CATALYTIC ACTIVITY: L-ornithine + a 2-oxo acid = L-glutamate 5-
semialdehyde + an L-amino acid. {ECO:0000256|HAMAP-Rule:MF_01689}.
-!- CATALYTIC ACTIVITY: N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-
acetyl-L-glutamate 5-semialdehyde + L-glutamate.
{ECO:0000256|HAMAP-Rule:MF_01107}.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000256|HAMAP-Rule:MF_01107};
Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000256|HAMAP-
Rule:MF_01107};
-!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-
acetyl-L-ornithine from L-glutamate: step 4/4. {ECO:0000256|HAMAP-
Rule:MF_01107}.
-!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-
glutamate 5-semialdehyde from L-ornithine: step 1/1.
{ECO:0000256|HAMAP-Rule:MF_01689}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01107}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01689}.
-!- MISCELLANEOUS: May also have succinyldiaminopimelate
aminotransferase activity, thus carrying out the corresponding
step in lysine biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01107}.
-!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
aminotransferase family. OAT subfamily. {ECO:0000256|HAMAP-
Rule:MF_01689}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KGR90247.1}.
-----------------------------------------------------------------------
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EMBL; JPVQ01000023; KGR90247.1; -; Genomic_DNA.
RefSeq; WP_036177424.1; NZ_JPVQ01000023.1.
EnsemblBacteria; KGR90247; KGR90247; CD30_12840.
UniPathway; UPA00068; UER00109.
UniPathway; UPA00098; UER00358.
Proteomes; UP000030595; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0003992; F:N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity; IEA:UniProtKB-UniRule.
GO; GO:0004587; F:ornithine-oxo-acid transaminase activity; IEA:UniProtKB-UniRule.
GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
CDD; cd00610; OAT_like; 1.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 2.
HAMAP; MF_01107; ArgD_aminotrans_3; 1.
HAMAP; MF_01689; Ornith_aminotrans_3; 1.
InterPro; IPR004636; AcOrn/SuccOrn_fam.
InterPro; IPR005814; Aminotrans_3.
InterPro; IPR010164; Orn_aminotrans.
InterPro; IPR034757; Ornith_aminotrans_bact.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
PANTHER; PTHR11986:SF94; PTHR11986:SF94; 1.
Pfam; PF00202; Aminotran_3; 1.
PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
SUPFAM; SSF53383; SSF53383; 1.
TIGRFAMs; TIGR01885; Orn_aminotrans; 1.
PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
3: Inferred from homology;
Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01107,
ECO:0000256|HAMAP-Rule:MF_01689};
Aminotransferase {ECO:0000256|HAMAP-Rule:MF_01689,
ECO:0000256|SAAS:SAAS00768889, ECO:0000313|EMBL:KGR90247.1};
Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01107};
Complete proteome {ECO:0000313|Proteomes:UP000030595};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01689};
Proline biosynthesis {ECO:0000256|HAMAP-Rule:MF_01689};
Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01689,
ECO:0000256|RuleBase:RU003560, ECO:0000256|SAAS:SAAS00768842};
Reference proteome {ECO:0000313|Proteomes:UP000030595};
Transferase {ECO:0000256|HAMAP-Rule:MF_01689,
ECO:0000256|SAAS:SAAS00768889, ECO:0000313|EMBL:KGR90247.1}.
REGION 108 109 Pyridoxal phosphate binding.
{ECO:0000256|HAMAP-Rule:MF_01107}.
REGION 228 231 Pyridoxal phosphate binding.
{ECO:0000256|HAMAP-Rule:MF_01107}.
BINDING 143 143 Pyridoxal phosphate; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_01107}.
BINDING 146 146 N2-acetyl-L-ornithine.
{ECO:0000256|HAMAP-Rule:MF_01107}.
BINDING 286 286 N2-acetyl-L-ornithine.
{ECO:0000256|HAMAP-Rule:MF_01107}.
BINDING 287 287 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_01107}.
MOD_RES 257 257 N6-(pyridoxal phosphate)lysine.
{ECO:0000256|HAMAP-Rule:MF_01689}.
SEQUENCE 398 AA; 43547 MW; 528729386F87F5E9 CRC64;
MTNATSSNLI EKTDKFGAHN YHPLPIVVSE AEGVWVKDPE GNKYMDMLSA YSALNQGHRH
PKIIKALIDQ ANRVTLTSRA FHNDQLGPWY EKLTQMTGKN MVLPMNTGAE AVESAIKVAR
RWAYEVKGVE DNKAEIIGCN GNFHGRTMGA VSLSSEKEYQ RGFGPILPGF KLIPYGDVES
LKAAITPNTA AFIVEPIQGE AGIVMPPKGF LKAAEQICKE NNVLFITDEI QTGLARTGKM
FAHQWDDVTP DVIILGKALG GGVMPISAVV ANSDILGVLN PGSHGSTFGG NPLACAVSLA
SLEVLEEENL TERSLELGNY FQEQLRGINN PVIKEVRGSG LFIGVELTEP ARKYCEQLME
KGLLCKETHD YVIRFAPPLI ISKEEIDWAL EHIQSIFA


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