ID A0A1C6UFH1_9ACTN Unreviewed; 770 AA.
AC A0A1C6UFH1;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Class II aldolase/adducin N-terminal domain-containing protein {ECO:0000259|SMART:SM01007};
GN ORFNames=GA0070617_2155 {ECO:0000313|EMBL:SCL52701.1};
OS Micromonospora yangpuensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=683228 {ECO:0000313|EMBL:SCL52701.1, ECO:0000313|Proteomes:UP000198937};
RN [1] {ECO:0000313|EMBL:SCL52701.1, ECO:0000313|Proteomes:UP000198937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45577 {ECO:0000313|EMBL:SCL52701.1,
RC ECO:0000313|Proteomes:UP000198937};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR EMBL; FMIA01000002; SCL52701.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C6UFH1; -.
DR STRING; 683228.GA0070617_2155; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000198937; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.225.10; Class II aldolase/adducin N-terminal domain; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR001303; Aldolase_II/adducin_N.
DR InterPro; IPR036409; Aldolase_II/adducin_N_sf.
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 PANTHER; PTHR43713; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE; 1.
DR PANTHER; PTHR43713:SF3; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE 1, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00596; Aldolase_II; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SMART; SM01007; Aldolase_II; 1.
DR SUPFAM; SSF53639; AraD/HMP-PK domain-like; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 4: Predicted;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000198937}.
FT DOMAIN 8..190
FT /note="Class II aldolase/adducin N-terminal"
FT /evidence="ECO:0000259|SMART:SM01007"
SQ SEQUENCE 770 AA; 82776 MW; 14E2A07B6F02DB54 CRC64;
MQHRTSRQHV VDMCRTMLDR GYLKATEGNV SVRVPGHRLY AVTPSNYDYD RMRVEDVCIV
DFAGRHVPDG SDVALKPSIE CGMHANIYRQ RPDVNAIVHT HQPYASALAV LRKPIPALSD
EQVRFLGRQV AIIDYAPSGT GLLARNVQKK VAGGDNAFII ANHGIVALGT DGDRAVFNMA
LLEKVSIAYL LALTTESGRV HTIPAAIREI AFGKLRADEK RIAAQLTEAV EPVRVPADEP
LPSADAKAAE IATGDHQATE IAGGDQQAAG TAAGEAVGTA AAGGAEAARL GYAISEYPDV
PDVMRRLKAL VAQPVRGLRH DAQLDVLDYF TTRCRASRAI TDRAKRRIPG GVQHNLAFNY
PFPLAIERAD GAYLVDRDGN TYIDFLQAGG PTILGSNYAP VNERVAEVVR ESGPVTGMFH
EYELKLAEII HRYLPHVEMY RSLGSGTEAV MAAVRGARAF TGKKMVIKVG GAYHGWSDTM
VYGLRVPGTY RMNAKGIPFG ATSRTREAFP HDLGQLRRKL IENRARGGTA AVIVEPVGPE
SGTRPVPRDF NARVRQLCDE FGALLIFDEV VTGFRLGLGG AAGYFGVTPD LTVLGKAVSG
GYPMAGGVGG RADVMAVFGS GLDGKSGAHI QVGGTLSANP LSCAAGYFAI EEMARTNAPV
IAGRAGDRLT RGLQRLIDSY GLPYVAYNQG SIVHLECSGV MLLDMRNPVK LLRENKARKR
LMEQMSAAYA AHGIITLAGS RMYTSMADTD EVIDDALARF DRVFALVEGV
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