ID D3AQH8_9CLOT Unreviewed; 373 AA.
AC D3AQH8;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Aminotransferase, acetylornithine/succinylornithine family {ECO:0000313|EMBL:EFC95930.1};
DE Flags: Fragment;
GN Name=argD {ECO:0000313|EMBL:EFC95930.1};
GN ORFNames=CLOSTHATH_05884 {ECO:0000313|EMBL:EFC95930.1};
OS Hungatella hathewayi DSM 13479.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Hungatella.
OX NCBI_TaxID=566550 {ECO:0000313|EMBL:EFC95930.1, ECO:0000313|Proteomes:UP000004968};
RN [1] {ECO:0000313|EMBL:EFC95930.1, ECO:0000313|Proteomes:UP000004968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13479 {ECO:0000313|EMBL:EFC95930.1,
RC ECO:0000313|Proteomes:UP000004968};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2010) 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. {ECO:0000256|ARBA:ARBA00029440}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {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:EFC95930.1}.
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DR EMBL; ACIO01000654; EFC95930.1; -; Genomic_DNA.
DR RefSeq; WP_006776301.1; NZ_GG667783.1.
DR AlphaFoldDB; D3AQH8; -.
DR HOGENOM; CLU_016922_10_1_9; -.
DR Proteomes; UP000004968; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProt.
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 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:0000313|EMBL:EFC95930.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:EFC95930.1}.
FT NON_TER 373
FT /evidence="ECO:0000313|EMBL:EFC95930.1"
SQ SEQUENCE 373 AA; 40726 MW; A623944B20330531 CRC64;
MPNKQEYIQK AEQEFYKTYN RFPVIFDHGD GVFLYDTEGE EYLDFGAGIA VMGLGYNDKE
YNEAVKTQVD KLLHTSNLFY NVPSIDAGEK LLAASGMDKV FFTNSGTEAI EGALKIARRY
AYNKAAGEKR GEGCVHEIIA MRHSFHGRSM GALSVTGNDH YQEPFKPLIP GIKFADFNDL
DSVKALVNEN TCAVIMETVQ GEGGIYPAEE EFLKGVRALC DEHSMLLILD EIQCGMGRTG
SMFAWQQYGV KPDVMTVAKA LGNGVPVGAF LASGKAAEAM VPGDHGTTYG GNPLVTAAAD
TVLSIFEKRG IVDHVNQIGG YLWKKLDELA DQFDCITGHR GMGLMQGLEF HMPVGPIVQK
ALLEEKLVLI SAG
//
