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Database: UniProt
Entry: A0A3E2N771_9CLOT
LinkDB: A0A3E2N771_9CLOT
Original site: A0A3E2N771_9CLOT 
ID   A0A3E2N771_9CLOT        Unreviewed;       415 AA.
AC   A0A3E2N771;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Starvation-sensing protein RspA {ECO:0000313|EMBL:RFZ76741.1};
GN   ORFNames=DS742_21850 {ECO:0000313|EMBL:RFZ76741.1};
OS   Clostridium indicum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=759821 {ECO:0000313|EMBL:RFZ76741.1, ECO:0000313|Proteomes:UP000260680};
RN   [1] {ECO:0000313|EMBL:RFZ76741.1, ECO:0000313|Proteomes:UP000260680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PI-S10-A1B {ECO:0000313|EMBL:RFZ76741.1,
RC   ECO:0000313|Proteomes:UP000260680};
RA   Krishna G., Summeta K., Shikha S., Prabhu P.B., Suresh K.;
RT   "New species, Clostridium PI-S10-A1B.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Has no detectable activity with D-mannonate and with a panel
CC       of 70 other acid sugars (in vitro), in spite of the conservation of the
CC       residues that are expected to be important for catalytic activity and
CC       cofactor binding. May have evolved a divergent function.
CC       {ECO:0000256|ARBA:ARBA00003553}.
CC   -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC       enzyme family. GalD subfamily. {ECO:0000256|ARBA:ARBA00010339}.
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:RFZ76741.1}.
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DR   EMBL; QOHO01000073; RFZ76741.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3E2N771; -.
DR   OrthoDB; 9775391at2; -.
DR   Proteomes; UP000260680; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR   GO; GO:0009063; P:amino acid catabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.120; Enolase-like C-terminal domain; 1.
DR   Gene3D; 3.30.390.10; Enolase-like, N-terminal domain; 1.
DR   InterPro; IPR034593; DgoD-like.
DR   InterPro; IPR036849; Enolase-like_C_sf.
DR   InterPro; IPR029017; Enolase-like_N.
DR   InterPro; IPR029065; Enolase_C-like.
DR   InterPro; IPR018110; Mandel_Rmase/mucon_lact_enz_CS.
DR   InterPro; IPR013342; Mandelate_racemase_C.
DR   InterPro; IPR013341; Mandelate_racemase_N_dom.
DR   PANTHER; PTHR48080; D-GALACTONATE DEHYDRATASE-RELATED; 1.
DR   PANTHER; PTHR48080:SF6; STARVATION-SENSING PROTEIN RSPA; 1.
DR   Pfam; PF13378; MR_MLE_C; 1.
DR   Pfam; PF02746; MR_MLE_N; 1.
DR   SMART; SM00922; MR_MLE; 1.
DR   SUPFAM; SSF51604; Enolase C-terminal domain-like; 1.
DR   SUPFAM; SSF54826; Enolase N-terminal domain-like; 1.
DR   PROSITE; PS00908; MR_MLE_1; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000260680}.
FT   DOMAIN          132..255
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
SQ   SEQUENCE   415 AA;  46423 MW;  FBAEA6057A0625FB CRC64;
     MDTKISDIQV ILTAPEGINL VVVKVITNQP GLYGLGCATF AYRHLAVKTV VEEYLKPLLT
     GREVDRIEDI WQLMHQNGYW RNGPIENNAI SGVDMALWDI KGKMAGMPVY QLFGGKCREG
     IPVYRHADGR DAEEVCDNIL RFKEMGITNI RCQCGGYGGD SYGTVPSTAP KGALSGVYLD
     SREYIQNTVK LFENIRNRIG YDMNLVHDVH ERIAPVDSIK LARALEPYDL FFLEDPVPIE
     QLPWLRNLRQ QTSIPIAEGE LFNHAVEWKQ IIAEHLIDFI RVHLSQIGGI TPARKLQIFA
     EQYGVRTAWH GPGDMSPIAH AANIHLDLSS PNFGVQEWSG IEPPNFVIQD LKGPRGALLE
     VFPGLPEFSD GYVYANDKPG LGVDINEKEA AKYPCESTVV TWTQTRRRDG ALQTP
//
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