ID A0A1A9GGB6_9ACTN Unreviewed; 556 AA.
AC A0A1A9GGB6;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Putative phosphomannomutase {ECO:0000313|EMBL:ANH36682.1};
DE EC=5.4.2.8 {ECO:0000313|EMBL:ANH36682.1};
GN ORFNames=I601_0229 {ECO:0000313|EMBL:ANH36682.1};
OS Nocardioides dokdonensis FR1436.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1300347 {ECO:0000313|EMBL:ANH36682.1, ECO:0000313|Proteomes:UP000077868};
RN [1] {ECO:0000313|EMBL:ANH36682.1, ECO:0000313|Proteomes:UP000077868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FR1436 {ECO:0000313|EMBL:ANH36682.1,
RC ECO:0000313|Proteomes:UP000077868};
RA Kwon S.-K., Kim K., Kim J.F.;
RT "Complete genome sequence of a soil Actinobacterium, Nocardioides
RT dokdonensis FR1436.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231, ECO:0000256|RuleBase:RU004326}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP015079; ANH36682.1; -; Genomic_DNA.
DR RefSeq; WP_068105332.1; NZ_CP015079.1.
DR AlphaFoldDB; A0A1A9GGB6; -.
DR STRING; 1300347.I601_0229; -.
DR KEGG; ndk:I601_0229; -.
DR PATRIC; fig|1300347.3.peg.229; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000077868; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd05799; PGM2; 1.
DR Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 3.
DR Gene3D; 3.30.310.50; Alpha-D-phosphohexomutase, C-terminal domain; 1.
DR InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
DR InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
DR InterPro; IPR005843; A-D-PHexomutase_C.
DR InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR PANTHER; PTHR45745:SF1; PHOSPHOGLUCOMUTASE 2A-RELATED; 1.
DR PANTHER; PTHR45745; PHOSPHOMANNOMUTASE 45A; 1.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 1.
DR Pfam; PF00408; PGM_PMM_IV; 1.
DR PRINTS; PR00509; PGMPMM.
DR SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:ANH36682.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004326};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000077868}.
FT DOMAIN 57..196
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 219..316
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 328..436
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 480..523
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 556 AA; 58017 MW; AE44A96F957178A2 CRC64;
MTSSAAPTDL LDRARAWADA DPDPGTRAEL EELLVAVESG DEAARADLAD RFDGTLEFGT
AGLRGAMGAG PNRMNRVVVT RAAAGLASYL VDQAEGGHAG RGAVVIGYDA RHLSEQFAQD
SAEVISGAGL DVWLLPRPLP TPVLAFAIQE LGCVAGVMVT ASHNPPQDNG YKVYLGDGSQ
IVPPADTQIA ERIAAVGELT SVPRAKGARV LDEEVVDSYL DTAAALAGDG PRDLDVVYTP
LHGVGGTTVA QVLETAGFAA PRMVEQQEQP DPEFSTVAFP NPEEEGAMDL ALELAARTDA
DLVVANDPDA DRCAAAVPTP TGWRMLRGDE VGALLGLHLV RRGVTGTLAT SIVSSSLLGK
IAAAAGLPYV ETLTGFKWIG RVEGLSFGYE EALGYCCDPE HVKDKDGVSA LLLLCEMAAE
AKAAGRSLLD LLDDLAQEHG LHATDQVSVR VEDVSLISDA MRRLRAQPPT VLGGLAVEGV
DDLAEGSADL PPTEGLRYRL ADGARVVVRP SGTEPKLKAY LEVVVPVRDE PVEAARIAAA
TRLDALAGDV RAALGL
//
