ID A4BU21_9GAMM Unreviewed; 841 AA.
AC A4BU21;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=phosphomannomutase {ECO:0000256|ARBA:ARBA00012730};
DE EC=5.4.2.8 {ECO:0000256|ARBA:ARBA00012730};
GN ORFNames=NB231_11214 {ECO:0000313|EMBL:EAR20842.1};
OS Nitrococcus mobilis Nb-231.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Nitrococcus.
OX NCBI_TaxID=314278 {ECO:0000313|EMBL:EAR20842.1, ECO:0000313|Proteomes:UP000003374};
RN [1] {ECO:0000313|EMBL:EAR20842.1, ECO:0000313|Proteomes:UP000003374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nb-231 {ECO:0000313|EMBL:EAR20842.1,
RC ECO:0000313|Proteomes:UP000003374};
RA Waterbury J., Ferriera S., Johnson J., Kravitz S., Halpern A.,
RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate;
CC Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735;
CC EC=5.4.2.8; Evidence={ECO:0000256|ARBA:ARBA00000586};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate:
CC step 2/2. {ECO:0000256|ARBA:ARBA00004699}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231}.
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:EAR20842.1}.
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DR EMBL; AAOF01000016; EAR20842.1; -; Genomic_DNA.
DR RefSeq; WP_005002583.1; NZ_CH672427.1.
DR AlphaFoldDB; A4BU21; -.
DR STRING; 314278.NB231_11214; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_013562_0_1_6; -.
DR OrthoDB; 9803322at2; -.
DR Proteomes; UP000003374; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd03089; PMM_PGM; 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; PTHR43771:SF2; PHOSPHOGLUCOMUTASE; 1.
DR PANTHER; PTHR43771; PHOSPHOMANNOMUTASE; 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};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000003374};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 29..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 265..286
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 392..520
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 536..633
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 638..747
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 776..831
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 841 AA; 90120 MW; FBDA163503626752 CRC64;
MKENGKRRAR PQDAPAATAP KGPKAITGYF ISVALVAVLL LLASLILTAA LGQRAKQALW
QAAANHTAEL ISRNLTAQIA TLYEALAETA RLEVLQKALQ NGDQSTLIEL TQVLQSALPP
AARLLIVPKG GLSPDPNATP PIGYALLDMV KVASAGHRPP AEVHLPGRPG ASVNLVEPVR
AGDAILGALV LTLPADRWFQ QLTPPPQAWI GLRRHSADAS VMLAESGNRQ AAGPRIRLAV
AGTAWQLEYI DGHSADPLAG MNTPLALTVV SAAILLILLS AVIVSVRLRR MLAADGQTFA
RIVQDCLTGK PQTHYTVRLR ELQAALTAAL SATRAPQTPI AAAGSPEESV EPAVDSERAA
KPVAAPQPME VAEINAAPHD FASAPPIDPS ILRAYNIRGT IGKTLTPEVV HWLGRAIGSE
AAARDQQTIV VGYDGRHSSP ELAKALNEGL AAAGRHIIDI GRVPTPVVYF ATYHLDSHAG
VIVTGSHNPP DYNGLKIVLG GESLSGEAIQ ALGRRIESGD LHLGRGGIER QDIFAAYRER
VLHDVALHRP LKVVVDCGNG VAGELAPDLI QALGCEVVEL FCEIDGDFPN HHPDPTAPEN
LESLIQQVHA QQADLGLAFD GDGDRLGVVD NQGKIIWPDR QLMLFAEDIL SRNPGSDIVF
DVKCTSRLAD VITEAAGVPI LWKTGHSLIK SKLRETGALL GGEMSGHIFF NDRWYGFDDA
IYAAARLLEI LSMDPRTSAE VFAQLPEAVS TPELRLDLEE GEPPRLMDTL RERASFGNAR
VTTIDGLRVD FPDGWGLVRA SNTQPCLVLR FEGDDTVALE RIETTFRELI ERVRPGLKLP
F
//
