ID A3TQJ1_9MICO Unreviewed; 550 AA.
AC A3TQJ1;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 85.
DE SubName: Full=Putative phosphomannomutase {ECO:0000313|EMBL:EAP97437.1};
GN ORFNames=JNB_18243 {ECO:0000313|EMBL:EAP97437.1};
OS Janibacter sp. HTCC2649.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Janibacter.
OX NCBI_TaxID=313589 {ECO:0000313|EMBL:EAP97437.1, ECO:0000313|Proteomes:UP000005063};
RN [1] {ECO:0000313|EMBL:EAP97437.1, ECO:0000313|Proteomes:UP000005063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2649 {ECO:0000313|EMBL:EAP97437.1,
RC ECO:0000313|Proteomes:UP000005063};
RX PubMed=21075932; DOI=10.1128/JB.01298-10;
RA Thrash J.C., Cho J.C., Bertagnolli A.D., Ferriera S., Johnson J.,
RA Vergin K.L., Giovannoni S.J.;
RT "Genome sequence of the Marine Janibacter Sp. Strain HTCC2649.";
RL J. Bacteriol. 193:584-585(2011).
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 -!- 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:EAP97437.1}.
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DR EMBL; AAMN01000004; EAP97437.1; -; Genomic_DNA.
DR RefSeq; WP_009777931.1; NZ_CH672413.1.
DR AlphaFoldDB; A3TQJ1; -.
DR STRING; 313589.JNB_18243; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_0_2_11; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000005063; Unassembled WGS sequence.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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};
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:UP000005063}.
FT DOMAIN 52..187
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 209..308
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 320..426
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 443..517
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 550 AA; 57539 MW; 3B421251E0B5FCF9 CRC64;
MNDDLVAAAR AWAADDPDPQ TKAELESVAD AASSGDPAAV EDLLDRMSGL LQFGTAGLRG
ALGGGPNRMN RSVVIRAAAG LTAYLKKTVA EPFVVIGFDA RFNSDVFARD TAAVVLGAGG
RASVLPRPLP TPVLAYAIRH LGADAGVMVT ASHNPPQDNG YKVYLGDGSQ IVSPSDVDIA
AEISRIERTL DVPLADDGWE TLDDEVLESY LTHVIDVVSP DTPRDLVVVH TALHGVGSET
VARAFVAAGY AAPLPVPSQA EPDPLFPTVP FPNPEEPGAM DAALELAEQT GPDVVIANDP
DADRCAVAVP GPGGWRMLRG DEVGVLLGAH LLERGVPADA VFANSIVSSR MLATVCRSVG
IAHEETLTGF KWISRVPGLR YGYEEALGYC VDPGQVRDKD GVSAALVVAE IAASLKASGG
SITERLDELA VTHGVHATDS FSVRVEDLAL IDQIMARLRA QTLSTVAGVE VSRVDDLAAG
DGGLPPTEGL RYFLADDSRV IVRPSGTEPK LKVYLEVIEA VSDGDLVGAR SRAGQRLSAI
RSDFEAATAL
//
