O57742 (APGM_PYRHO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
2,3-bisphosphoglycerate-independent phosphoglycerate mutase
Short name=BPG-independent PGAM
Short name=Phosphoglyceromutase
Short name=aPGAM
EC=5.4.2.1

Gene names

Name:	apgM
Ordered Locus Names:	PH0037

Organism

Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) [Complete proteome] [HAMAP]

Taxonomic identifier

70601 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length	412 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate By similarity. HAMAP MF_01402_A
Catalytic activity	2-phospho-D-glycerate = 3-phospho-D-glycerate. HAMAP MF_01402_A
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. HAMAP MF_01402_A
Sequence similarities	Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.

Ontologies

Keywords
Biological process	Glycolysis
Molecular function	Isomerase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	metal ion binding Inferred from electronic annotation. Source: InterPro phosphoglycerate mutase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 412

412

2,3-bisphosphoglycerate-independent phosphoglycerate mutase HAMAP MF_01402_A

PRO_0000138145

Secondary structure

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412

Helix Strand Turn

Details...

Beta strand

8 – 12

5

Helix

21 – 23

3

Helix

28 – 31

4

Helix

35 – 42

8

Helix

61 – 67

7

Helix

72 – 75

4

Turn

82 – 84

3

Beta strand

122 – 124

3

Helix

131 – 135

5

Helix

139 – 142

4

Helix

238 – 242

5

Turn

253 – 255

3

Turn

259 – 261

3

Helix

280 – 293

14

Beta strand

295 – 301

7

Helix

303 – 306

4

Helix

313 – 326

14

Helix

330 – 332

3

Turn

336 – 338

3

Beta strand

339 – 344

6

Turn

351 – 353

3

Beta strand

364 – 366

3

Turn

381 – 384

4

Helix

396 – 403

8

Sequences

	Sequence		Length	Mass (Da)
	O57742 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: E10944A6762DF6D4	FASTA	412	45,420
	10 20 30 40 50 60 MVLKRKGLLI ILDGLGDRPI KELNGLTPLE YANTPNMDKL AEIGILGQQD PIKPGQPAGS 70 80 90 100 110 120 DTAHLSIFGY DPYETYRGRG FFEALGVGLD LSKDDLAFRV NFATLENGII TDRRAGRIST 130 140 150 160 170 180 EEAHELARAI QEEVDIGVDF IFKGATGHRA VLVLKGMSRG YKVGDNDPHE AGKPPLKFSY 190 200 210 220 230 240 EDEDSKKVAE ILEEFVKKAQ EVLEKHPINE RRRKEGKPIA NYLLIRGAGT YPNIPMKFTE 250 260 270 280 290 300 QWKVKAAGVI AVALVKGVAR AVGFDVYTPE GATGEYNTNE MAKAKKAVEL LKDYDFVFLH 310 320 330 340 350 360 FKPTDAAGHD NKPKLKAELI ERADRMIGYI LDHVDLEEVV IAITGDHSTP CEVMNHSGDP 370 380 390 400 410 VPLLIAGGGV RTDDTKRFGE REAMKGGLGR IRGHDIVPIM MDLMNRSEKF GA

References

[1]

"Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3." Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T. , Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H. DNA Res. 5:55-76(1998) [PubMed: 9679194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BA000001 Genomic DNA. Translation: BAA29105.1.

PIR

B71222.

RefSeq

NP_142058.1. NC_000961.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2ZKT	X-ray	2.40	A/B	1-412	[»]

ProteinModelPortal

O57742.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBPYRT00000000007; EBPYRP00000000007; EBPYRG00000000007.

GeneID

1443938.

GenomeReviews

Gene locus PH0037 in contig BA000001_GR.

KEGG

pho:PH0037.

NMPDR

fig|70601.1.peg.38.

Organism-specific databases

CMR

Search...

Phylogenomic databases

GeneTree

EBGT00050000023120.

HOGENOM

HBG463247.

OMA

DIAFRCN.

ProtClustDB

PRK04024.

Enzyme and pathway databases

BioCyc

PHOR70601:PH0037-MONOMER.

Family and domain databases

HAMAP

MF_01402_A. ApgM_A.
[Tree]

InterPro

IPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR023665. ApgAM.
IPR004456. BisP-indep_Pglycerate_Mutase.
IPR006124. Metalloenzyme.
[Graphical view]

Gene3D

G3DSA:3.40.720.10. Alk_phosphtse. 2 hits.

KO

K15635.

Pfam

PF01676. Metalloenzyme. 1 hit.
PF10143. PhosphMutase. 1 hit.
[Graphical view]

PIRSF

PIRSF006392. IPGAM_arch. 1 hit.

SUPFAM

SSF53649. Alkaline_phosphatase_core. 1 hit.

TIGRFAMs

TIGR00306. ApgM. 1 hit.

ProtoNet

Search...

Entry information

Entry name

APGM_PYRHO

Accession

Primary (citable) accession number: O57742

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2002
Last sequence update:	August 1, 1998
Last modified:	January 25, 2012
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program