ID A4EGF8_9RHOB Unreviewed; 382 AA.
AC A4EGF8;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Putative FlmB {ECO:0000313|EMBL:EBA13980.1};
GN ORFNames=RCCS2_08824 {ECO:0000313|EMBL:EBA13980.1};
OS Roseobacter sp. CCS2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseobacter.
OX NCBI_TaxID=391593 {ECO:0000313|EMBL:EBA13980.1, ECO:0000313|Proteomes:UP000003535};
RN [1] {ECO:0000313|EMBL:EBA13980.1, ECO:0000313|Proteomes:UP000003535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCS2 {ECO:0000313|EMBL:EBA13980.1,
RC ECO:0000313|Proteomes:UP000003535};
RA Mary Ann M.A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
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:EBA13980.1}.
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DR EMBL; AAYB01000001; EBA13980.1; -; Genomic_DNA.
DR RefSeq; WP_008232071.1; NZ_AAYB01000001.1.
DR AlphaFoldDB; A4EGF8; -.
DR eggNOG; COG0399; Bacteria.
DR OrthoDB; 9768668at2; -.
DR Proteomes; UP000003535; Unassembled WGS sequence.
DR CDD; cd00616; AHBA_syn; 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; IPR000653; DegT/StrS_aminotransferase.
DR InterPro; IPR020026; PseC.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR03588; PseC; 1.
DR PANTHER; PTHR30244:SF45; LIPOPOLYSACCHARIDE BIOSYNTHESIS PROTEIN RFBH; 1.
DR PANTHER; PTHR30244; TRANSAMINASE; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR PIRSF; PIRSF000390; PLP_StrS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508}.
FT ACT_SITE 188
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 188
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 382 AA; 41903 MW; 2F9C94BE95F8BF6F CRC64;
MIPYGRQIIN DDDIAAVAAV LRSDFLTQGP VVPRFEDAVA DRVGAQHAVA VNSATSALHI
ACLALDLGPG DLLWTSPITF VASANCGRYC GADVDFVDID PGTFNICADA LEAKINQAAS
DGRLPKVIVA VHMCGQSPDM LRISELARRH GIRLIEDASH SIGADYRNAP VGNCAYSDIT
VFSFHPVKII TTAEGGMALT NNADLAARMQ RLRSHGITRD ENLMTHASDG PWYYQQIELG
WNYRMTELHA ALGLSQLGRL DDFVTRRNAL ADRYDALLAD LPLNLPKRLI DARASFHLYV
VRLHDEARHR SVFEALRSDG IGVNLHYIPV HLQPYYRDLG FADGDFPVSE DYYKRAVSIP
LHAGLSEAEQ DTVVACLKRA LA
//
