ID X1T5D6_9ZZZZ Unreviewed; 305 AA.
AC X1T5D6;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Metalloenzyme domain-containing protein {ECO:0000259|Pfam:PF01676};
DE Flags: Fragment;
GN ORFNames=S12H4_19291 {ECO:0000313|EMBL:GAI82820.1};
OS marine sediment metagenome.
OC unclassified sequences; metagenomes; ecological metagenomes.
OX NCBI_TaxID=412755 {ECO:0000313|EMBL:GAI82820.1};
RN [1] {ECO:0000313|EMBL:GAI82820.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Expedition CK06-06 {ECO:0000313|EMBL:GAI82820.1};
RX PubMed=24624126; DOI=10.3389/fmicb.2014.00080;
RA Kawai M., Futagami T., Toyoda A., Takaki Y., Nishi S., Hori S., Arai W.,
RA Tsubouchi T., Morono Y., Uchiyama I., Ito T., Fujiyama A., Inagaki F.,
RA Takami H.;
RT "High frequency of phylogenetically diverse reductive dehalogenase-
RT homologous genes in deep subseafloor sedimentary metagenomes.";
RL Front. Microbiol. 5:80-80(2014).
CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC phosphoglycerate. {ECO:0000256|ARBA:ARBA00002315}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate;
CC Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC EC=5.4.2.12; Evidence={ECO:0000256|ARBA:ARBA00000370};
CC -!- PATHWAY: Carbohydrate degradation. {ECO:0000256|ARBA:ARBA00004921}.
CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC family. A-PGAM subfamily. {ECO:0000256|ARBA:ARBA00005524}.
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:GAI82820.1}.
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DR EMBL; BARW01009630; GAI82820.1; -; Genomic_DNA.
DR AlphaFoldDB; X1T5D6; -.
DR GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR CDD; cd16011; iPGM_like; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR Gene3D; 3.30.70.2130; Metalloenzyme domain; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR006124; Metalloenzyme.
DR InterPro; IPR004456; Pglycerate_mutase_ApgM.
DR InterPro; IPR042253; Pglycerate_mutase_ApgM_sf.
DR PANTHER; PTHR31209; COFACTOR-INDEPENDENT PHOSPHOGLYCERATE MUTASE; 1.
DR PANTHER; PTHR31209:SF0; METALLOENZYME DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01676; Metalloenzyme; 1.
DR Pfam; PF10143; PhosphMutase; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE 3: Inferred from homology;
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152}.
FT DOMAIN 191..305
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:GAI82820.1"
FT NON_TER 305
FT /evidence="ECO:0000313|EMBL:GAI82820.1"
SQ SEQUENCE 305 AA; 33563 MW; 1BEC39BC0F07BAD0 CRC64;
CWETLASGTA LAREAVKQIR EGAKESVCGL IDPVSLGITP GSAPGHLAIF GYDPIKYNIG
RGIIEALGID LELKPEDIAA RGNFCTIDNR GIITDRRAGR ITTEKNAELC QLLNKIAIDG
VEILVAPVKE HRFVLILRGG GLSWELTDSD PQQVGLAPKK IEALLPQAQR TAEIANEFVS
QARTCLKNES LANMVLMRGF SQRPDIPFIP EIYKLKPAAI AIYPMYRGLA RLVGMQILPA
GGSITDQLER LHYHYKDYDF FFIHFKATDS RGEDGDFEAK VRAIEEVDAA LPNLLKLNPD
VLIVT
//
