ID M1NZS8_BARAA Unreviewed; 542 AA.
AC M1NZS8;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent) {ECO:0000256|ARBA:ARBA00012728};
DE EC=5.4.2.2 {ECO:0000256|ARBA:ARBA00012728};
GN Name=pgm {ECO:0000313|EMBL:AGF74917.1};
GN OrderedLocusNames=BAnh1_10480 {ECO:0000313|EMBL:AGF74917.1};
OS Bartonella australis (strain Aust/NH1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=1094489 {ECO:0000313|EMBL:AGF74917.1, ECO:0000313|Proteomes:UP000011729};
RN [1] {ECO:0000313|EMBL:AGF74917.1, ECO:0000313|Proteomes:UP000011729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Aust/NH1 {ECO:0000313|EMBL:AGF74917.1,
RC ECO:0000313|Proteomes:UP000011729};
RX PubMed=23555299; DOI=10.1371/journal.pgen.1003393;
RA Guy L., Nystedt B., Toft C., Zaremba-Niedzwiedzka K., Berglund E.C.,
RA Granberg F., Naslund K., Eriksson A.S., Andersson S.G.;
RT "A gene transfer agent and a dynamic repertoire of secretion systems hold
RT the keys to the explosive radiation of the emerging pathogen Bartonella.";
RL PLoS Genet. 9:E1003393-E1003393(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate;
CC Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601;
CC EC=5.4.2.2; Evidence={ECO:0000256|ARBA:ARBA00000443};
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}.
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DR EMBL; CP003123; AGF74917.1; -; Genomic_DNA.
DR RefSeq; WP_015398421.1; NC_020300.1.
DR AlphaFoldDB; M1NZS8; -.
DR STRING; 1094489.BAnh1_10480; -.
DR KEGG; baus:BAnh1_10480; -.
DR PATRIC; fig|1094489.3.peg.1290; -.
DR eggNOG; COG0033; Bacteria.
DR HOGENOM; CLU_009330_0_1_5; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000011729; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR InterPro; IPR045244; PGM.
DR PANTHER; PTHR22573:SF2; PHOSPHOGLUCOMUTASE; 1.
DR PANTHER; PTHR22573; PHOSPHOHEXOMUTASE FAMILY MEMBER; 1.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 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 Magnesium {ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|RuleBase:RU004326};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 14..151
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 184..286
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 295..407
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 542 AA; 59624 MW; 96092549C957D4ED CRC64;
MTVTTVSTTA FDDQKPGTSG LRKKVSVFQQ PHYVENFIQS IFNNVGSFEG KLLILGGDGR
YLNRTLIQTV LKMAAANGVG YVKVGRGGIL STPAVSHLIR KYNAHGGIIL SASHNPGGPN
GDCGIKYNIS NGGPAPNSLC DAIFTTSQRL SSYKIVEAPE IDLEVEAKTV IESMQVEIID
PVVDYVSLMQ EIFDFDCIAQ AVSKGLTLRF DAMHAVTGPY AQEIFEKHLG FPQGTVINSV
PLPDFGGGHP DPNLVYAKDL YRLLMSDRGP DLGAASDGDG DRNLIIGRKQ FVTPSDSLAI
MTAHAPLIKG YRQGIAGIAR SMPTGRAVDR VAEEEGLNCF ETPTGWKFFG TLLDAGKVTF
CGEESFGTGS NHVREKDGLW AVLFWLNLLA ATGETVAQIA QRHWRRYGRF YYLRCDYEEV
DTPKAHAMMD QLRAQLPEAG TKIGGLTVKK ADDFIYHDPI DQTITMQQGV RIFFDHDARI
VVRLSGTGTK GTTVRLYFEQ YENDPCKHDQ EPQKVIQPLQ RAALELLNIK KYLGREQPDI
IT
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