ID A0A317X3J5_9EURO Unreviewed; 474 AA.
AC A0A317X3J5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=acetylornithine transaminase {ECO:0000256|ARBA:ARBA00012919};
DE EC=2.6.1.11 {ECO:0000256|ARBA:ARBA00012919};
GN ORFNames=BO94DRAFT_533694 {ECO:0000313|EMBL:PWY91548.1};
OS Aspergillus sclerotioniger CBS 115572.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450535 {ECO:0000313|EMBL:PWY91548.1, ECO:0000313|Proteomes:UP000246702};
RN [1] {ECO:0000313|EMBL:PWY91548.1, ECO:0000313|Proteomes:UP000246702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115572 {ECO:0000313|EMBL:PWY91548.1,
RC ECO:0000313|Proteomes:UP000246702};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 4/4.
CC {ECO:0000256|ARBA:ARBA00005024}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC ECO:0000256|RuleBase:RU003560}.
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:PWY91548.1}.
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DR EMBL; MSFK01000009; PWY91548.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317X3J5; -.
DR STRING; 1450535.A0A317X3J5; -.
DR OrthoDB; 5487467at2759; -.
DR UniPathway; UPA00068; UER00109.
DR Proteomes; UP000246702; Unassembled WGS sequence.
DR GO; GO:0003992; F:N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
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; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Aminotransferase {ECO:0000313|EMBL:PWY91548.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000246702};
KW Transferase {ECO:0000313|EMBL:PWY91548.1}.
SQ SEQUENCE 474 AA; 50763 MW; 1179A3D7B72DA444 CRC64;
MAFIHLAARR LPVTRRLVPG IDSLAQQRLF SVSRQVSSQA KASVPNPDPA ADSASVAFVN
DQIPYMVPTY VRPAPVMVKG QGAYLWDMEN RKYLDLTAGI AVNSLGHCDP EVAQIISEQA
EVLVHASNLY YNAWTGALSK LLIDVTHKSG AMRDASQVFI CNSGTEANEA AIKFARKVGR
SHDPSGAKHE IVSFHNSFHG RTMGALSATP NPKYQTPFSP MLPGFKYGKY NDVAQLETLI
TEKTCGVIVE PIQGEGGINV GTPEFLTALR KRCDEVGAVL IFDEIQCGLS RTGTFWAHAH
PSLAPASGEA AHPDILTSAK ALGNGVPIGA TIVSEKAVAR HIKPGDHGTT YGGNPLVCRV
AHHIVNRLAS PELQRGVEAK GAFLVSGFEA LQKKYPNVIS EIRGRGLILG VQLSPEFTAK
ASDLVAAARE RGMLIITAGE GCIRFVPPLT ITEEQLKTGL RILEQALEAV VTAA
//
