ID D8PH31_9BACT Unreviewed; 425 AA.
AC D8PH31;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE SubName: Full=Putative Aminotransferase {ECO:0000313|EMBL:CBK42568.1};
DE EC=2.6.1.- {ECO:0000313|EMBL:CBK42568.1};
GN ORFNames=NIDE2865 {ECO:0000313|EMBL:CBK42568.1};
OS Nitrospira defluvii.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Nitrospira.
OX NCBI_TaxID=330214 {ECO:0000313|EMBL:CBK42568.1, ECO:0000313|Proteomes:UP000001660};
RN [1] {ECO:0000313|EMBL:CBK42568.1, ECO:0000313|Proteomes:UP000001660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20624973; DOI=10.1073/pnas.1003860107;
RA Lucker S., Wagner M., Maixner F., Pelletier E., Koch H., Vacherie B.,
RA Rattei T., Sinninghe Damste J., Spieck E., Le Paslier D., Daims H.;
RT "A Nitrospira metagenome illuminates the physiology and evolution of
RT globally important nitrite-oxidizing bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 0:13479-13484(2010).
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
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DR EMBL; FP929003; CBK42568.1; -; Genomic_DNA.
DR AlphaFoldDB; D8PH31; -.
DR STRING; 330214.NIDE2865; -.
DR KEGG; nde:NIDE2865; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_036177_0_0_0; -.
DR OrthoDB; 9804264at2; -.
DR Proteomes; UP000001660; Chromosome.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; IPR000653; DegT/StrS_aminotransferase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR30244:SF34; DTDP-4-AMINO-4,6-DIDEOXYGALACTOSE TRANSAMINASE; 1.
DR PANTHER; PTHR30244; TRANSAMINASE; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 2.
DR PIRSF; PIRSF000390; PLP_StrS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:CBK42568.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000001660};
KW Transferase {ECO:0000313|EMBL:CBK42568.1}.
FT ACT_SITE 182
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 182
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 425 AA; 46513 MW; E91F143A50DB9667 CRC64;
MKAQRTLPPA AAPIEWRDLI QGLMGLVHPH ETVGRLQAEF RQYFGVKHVW FVSSGKAALS
LIFQALHSLS GRSKVVLPGY TCFSVPSAVV RARLSVALCD VDPLSLDFDF VQLSQVADSN
VLCVLATHLL GIGVDVPRVV ELCRQRGIFV VEDVAQAFGG KRDGVPFGAM GDVSFLSFGR
GKNITCGSGG AILTNDDRIG EVLAREYALL SEVSLADMLK NWLEVAVTKV LLNPSLYWLP
AGLPFLKLGE TKFYTDFPIA RLDPIRAGLL RRWKRRLANS TTSRVAHSEQ ILRSLALSNV
QTIKPSGRGR SVYLRLPVLM GSRQEKDAVC RISAEQGLGI SPLYPSSLQH IAELIDTLSS
QDVPQSTMIA ERLVTLPTHE LVSDSDVVRI SSIIQAAERV DGAATIRRPN ITNGQRHVPE
LPRNI
//
