ID M1WMM1_PSEP2 Unreviewed; 388 AA.
AC M1WMM1;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Spore coat polysaccharide biosynthesis protein spsC {ECO:0000313|EMBL:CCH49795.1};
GN Name=spsC {ECO:0000313|EMBL:CCH49795.1};
GN OrderedLocusNames=BN4_12560 {ECO:0000313|EMBL:CCH49795.1};
OS Pseudodesulfovibrio piezophilus (strain DSM 21447 / JCM 15486 / C1TLV30)
OS (Desulfovibrio piezophilus).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae.
OX NCBI_TaxID=1322246 {ECO:0000313|EMBL:CCH49795.1, ECO:0000313|Proteomes:UP000011724};
RN [1] {ECO:0000313|EMBL:CCH49795.1, ECO:0000313|Proteomes:UP000011724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10523 / SB164P1 {ECO:0000313|Proteomes:UP000011724};
RX PubMed=23383081; DOI=10.1371/journal.pone.0055130;
RA Pradel N., Ji B., Gimenez G., Talla E., Lenoble P., Garel M., Tamburini C.,
RA Fourquet P., Lebrun R., Bertin P., Denis Y., Pophillat M., Barbe V.,
RA Ollivier B., Dolla A.;
RT "The first genomic and proteomic characterization of a deep-sea sulfate
RT reducer: insights into the piezophilic lifestyle of Desulfovibrio
RT piezophilus.";
RL PLoS ONE 8:e55130-e55130(2013).
RN [2] {ECO:0000313|Proteomes:UP000011724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10523 / SB164P1 {ECO:0000313|Proteomes:UP000011724};
RX PubMed=23961312; DOI=10.4056/sigs.3777412;
RA Finster K.W., Kjeldsen K.U., Kube M., Reinhardt R., Mussmann M., Amann R.,
RA Schreiber L.;
RT "Complete genome sequence of Desulfocapsa sulfexigens, a marine
RT deltaproteobacterium specialized in disproportionating inorganic sulfur
RT compounds.";
RL Stand. Genomic Sci. 8:58-68(2013).
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
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DR EMBL; FO203427; CCH49795.1; -; Genomic_DNA.
DR RefSeq; WP_015415838.1; NC_020409.1.
DR AlphaFoldDB; M1WMM1; -.
DR STRING; 1322246.BN4_12560; -.
DR KEGG; dpi:BN4_12560; -.
DR PATRIC; fig|879567.3.peg.2745; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_7_2_7; -.
DR OrthoDB; 9766188at2; -.
DR BioCyc; DPIE1322246:BN4_RS12860-MONOMER; -.
DR Proteomes; UP000011724; Chromosome.
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; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000011724}.
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 388 AA; 42843 MW; FF93DD61A055AEBF CRC64;
MPVRSKNNFL IFGSPRIEQD EIDEVVASME AGWLGTGPKV AKFESDFATY LGSGHAAACN
SCTAALHLGL VALGLKPGDE VITTPLTFCA SVNAIIHAGC TPVLADVDPV SMNIDPESIR
AKITKRTKAI LPVHFAGRAC DMDAIMSIAT EHDLKVVEDC AHAIETTYKG QHVGTFGNFG
CFSFYVTKNV CTGEGGMVMA NSEEDIKHVK ILGLHGMSAD AWKRFSDDGY KHYQVVEAGF
KYNMMDIQAA IGIHQLKRVE EYHVRRRHVW DMYMDAFKAL PIGLPAPEEP DTRHALHLFT
ILIDPDSCGV ERDEFLIRMT HENIGVGVHY LSIPEQPYYR ERFGWTLEDT PHAVRLGRQT
VSLPLSAKLT DQDVLDVIQA VKKSLAIS
//
