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Database: UniProt
Entry: A0A1Q9LRW2_9PSEU
LinkDB: A0A1Q9LRW2_9PSEU
Original site: A0A1Q9LRW2_9PSEU 
ID   A0A1Q9LRW2_9PSEU        Unreviewed;       316 AA.
AC   A0A1Q9LRW2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Putative gluconeogenesis factor {ECO:0000256|HAMAP-Rule:MF_00973};
GN   ORFNames=BJP25_12975 {ECO:0000313|EMBL:OLR94776.1};
OS   Actinokineospora bangkokensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Actinokineospora.
OX   NCBI_TaxID=1193682 {ECO:0000313|EMBL:OLR94776.1, ECO:0000313|Proteomes:UP000186040};
RN   [1] {ECO:0000313|EMBL:OLR94776.1, ECO:0000313|Proteomes:UP000186040}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=44EHW {ECO:0000313|EMBL:OLR94776.1,
RC   ECO:0000313|Proteomes:UP000186040};
RA   Greule A., Intra B., Flemming S., Rommel M.G., Panbangred W., Bechthold A.;
RT   "The Draft Genome Sequence of Actinokineospora bangkokensis 44EHWT reveals
RT   the biosynthetic pathway of antifungal compounds Thailandins with unusual
RT   extender unit butylmalonyl-CoA.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for morphogenesis under gluconeogenic growth
CC       conditions. {ECO:0000256|HAMAP-Rule:MF_00973}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00973}.
CC   -!- SIMILARITY: Belongs to the gluconeogenesis factor family.
CC       {ECO:0000256|HAMAP-Rule:MF_00973}.
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:OLR94776.1}.
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DR   EMBL; MKQR01000007; OLR94776.1; -; Genomic_DNA.
DR   RefSeq; WP_075974155.1; NZ_MKQR01000007.1.
DR   AlphaFoldDB; A0A1Q9LRW2; -.
DR   STRING; 1193682.BJP25_12975; -.
DR   OrthoDB; 9783842at2; -.
DR   Proteomes; UP000186040; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043743; F:LPPG:FO 2-phospho-L-lactate transferase activity; IEA:InterPro.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-UniRule.
DR   CDD; cd07187; YvcK_like; 1.
DR   Gene3D; 3.40.50.10680; CofD-like domains; 1.
DR   HAMAP; MF_00973; Gluconeogen_factor; 1.
DR   InterPro; IPR002882; CofD.
DR   InterPro; IPR038136; CofD-like_dom_sf.
DR   InterPro; IPR010119; Gluconeogen_factor.
DR   NCBIfam; TIGR01826; CofD_related; 1.
DR   PANTHER; PTHR30135:SF3; GLUCONEOGENESIS FACTOR-RELATED; 1.
DR   PANTHER; PTHR30135; UNCHARACTERIZED PROTEIN YVCK-RELATED; 1.
DR   Pfam; PF01933; CofD; 1.
DR   SUPFAM; SSF142338; CofD-like; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00973};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186040}.
SQ   SEQUENCE   316 AA;  32432 MW;  9770FC83450FCFA2 CRC64;
     MRAVALGGGH GLHATLTALR AVTPDVTAVV TVADDGGSSG RLRRELGLLP PGDLRKALLA
     LAGPDTGPWG EVFGHRFGGT GALAGHAVGN LVLAGLLETV GDPVAVLAEA ARLLGVRGRV
     LPMSPEPVDI EADVTGLGAD PAAISRIRGQ VAVATTPGRV RRIRLCAADR RSEPPKACAE
     AVEAVLGADV VLLGPGSWFT SVLPHLLVPD LHDALVRTAA RRVVVLNLVP QPGETEGFSP
     EHHLDVLVEH APSLRVDAVV ADADSVPTPE RLRQAAAALG AELRLDRVAA PDAADRHDTA
     ALSASLARAV ATAARR
//
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