ID A0A094HYK0_9PEZI Unreviewed; 474 AA.
AC A0A094HYK0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=acetylornithine transaminase {ECO:0000256|ARBA:ARBA00012919};
DE EC=2.6.1.11 {ECO:0000256|ARBA:ARBA00012919};
GN ORFNames=V502_06690 {ECO:0000313|EMBL:KFZ13311.1};
OS Pseudogymnoascus sp. VKM F-4520 (FW-2644).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420915 {ECO:0000313|EMBL:KFZ13311.1, ECO:0000313|Proteomes:UP000029308};
RN [1] {ECO:0000313|EMBL:KFZ13311.1, ECO:0000313|Proteomes:UP000029308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4520 (FW-2644) {ECO:0000313|Proteomes:UP000029308};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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:KFZ13311.1}.
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DR EMBL; JPKE01002454; KFZ13311.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094HYK0; -.
DR STRING; 1420915.A0A094HYK0; -.
DR HOGENOM; CLU_016922_10_1_1; -.
DR OrthoDB; 5487467at2759; -.
DR UniPathway; UPA00068; UER00109.
DR Proteomes; UP000029308; 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; IPR049704; Aminotrans_3_PPA_site.
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};
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000029308};
KW Transferase {ECO:0000256|ARBA:ARBA00022576}.
SQ SEQUENCE 474 AA; 49895 MW; 76D25410E846B4E8 CRC64;
MSMSLRISAR RAAAASLKMS NAPARRSASQ AAAAASGSNL PEQLKNEIFK AAHLPNPDPA
EDSATTTVVN EQAPYMVKTY ARPAPMFVKG QGSYLYDLEN RKYLDFTAGI AVNALGHCDP
EISELIYSQA KTLVHTSNLY HNPWTGALST LLVQKTLESG GMSGVSSVFI CNSGSEANEA
AIKFARKAGK VADPSGAKHE IVSFYNSFHG RTMGSLSATP NPKYQAPFAP MLPGFRYGTY
NDIAGIAELV TPATAGVIVE PIQGEGGVHV ATPEFLIALA ARCKEVGALL IYDEIQCGLS
RTGTLWAHSE LPASAHPDIL TTAKALGNGF PVGATLVTGS VAEKIAVGDH GTTFGGNPLA
SRLAHHIVSR LSQPELQEAV AAKSALFVGH MKKLQEKYPK LVGEIRGKGL LLGLQLDRDP
TPIVAAARER GLLVITAGTN TLRFVPPLTI SEAEIEEGFA VLDAVMGVVA AGDN
//