Reviewed, UniProtKB/Swiss-Prot P43799 (GLPA_HAEIN)

Names and origin

Protein names

Recommended name:
    Anaerobic glycerol-3-phosphate dehydrogenase subunit A
      Short name=G-3-P dehydrogenase
    EC=1.1.5.3

Gene names

Name:	glpA
Ordered Locus Names:	HI0685

Organism

Haemophilus influenzae [Complete proteome] [HAMAP]

Taxonomic identifier

727 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length	563 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol.
Cofactor	FAD By similarity. FMN By similarity.
Pathway	Polyol metabolism; glycerol degradation via glycerol kinase pathway; glycerone phosphate from sn-glycerol 3-phosphate (anaerobic route): step 1/1.
Subunit structure	Composed of a catalytic glpA/B dimer and of membrane bound glpC By similarity.
Subcellular location	Cell inner membrane; Peripheral membrane protein By similarity. Note: Loosely bound to the cytoplasmic membrane often occurring in vesicles associated with fumarate reductase By similarity.
Sequence similarities	Belongs to the FAD-dependent glycerol-3-phosphate dehydrogenase family.

Ontologies

Keywords
Cellular component	Cell inner membrane Cell membrane Membrane
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glycerol-3-phosphate metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW polyol catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	glycerol-3-phosphate dehydrogenase complex Inferred from electronic annotation. Source: InterPro plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro FMN binding Inferred from electronic annotation. Source: InterPro glycerol-3-phosphate dehydrogenase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 563	563	Anaerobic glycerol-3-phosphate dehydrogenase subunit A		PRO_0000126095
Regions
	Nucleotide binding	20 – 48	29	FAD Potential

Sequences

	Sequence		Length	Mass (Da)
	P43799-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 7E662A80F4E1EED6	FASTA	563	61,920
	10 20 30 40 50 60 MGLSPSIYKD VGDLSSLSTD VIIIGGGATG AGIARDCALR GIDCILLERR DIATGATGRN 70 80 90 100 110 120 HGLLHSGARY AVNDQESAEE CIKENRILRK IARHCVDETE GLFITLPEDS LDYQKTFLES 130 140 150 160 170 180 CAKSGIDAQA IDPELAKIME PSVNPDLVGA VVVPDGSIDP FRLTASNMMD ATENGAKMFT 190 200 210 220 230 240 YCEVKNLIRE GGKVIGVNAY DHKNRRERQF FAPLVVNAGG IWGQGIAEYA DLKIKMFPAK 250 260 270 280 290 300 GALLVMGHRI NKLVINRCRK PADADILVPG DTICVIGTTS SRIPYDQIDN MEVTPEEVDI 310 320 330 340 350 360 LFREGEKLAP SLRHTRVLRA YAGVRPLVAS DDDPSGRNVS RGIVLLDHAE RDGLDGFITI 370 380 390 400 410 420 TGGKLMTYRL MAEWATDLVC KKLNKTARCV TAEQPLPGST ESRQETNQKV ISLPSTIRYS 430 440 450 460 470 480 AVYRHGSRAT RLLEKERLDR SMVCECEAVT AGEVRYAVDE LDVNNLVDLR RRSRVGMGTC 490 500 510 520 530 540 QAELCACRAA GLMNRFEVAT PRQSTTQLSA FMEERWRGIE PIAWGEAIRE AEFTSWMYAS 550 560 VLGLNDVKPL DEQAQQGTDS NEF

References

[1]

"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed: 7542800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L42023 Genomic DNA. Translation: AAC22345.1.
PIR	E64086.
RefSeq	NP_438845.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	949605.
GenomeReviews	Gene locus HI0685 in contig L42023_GR.
KEGG	hin:HI0685.
NMPDR	fig|71421.1.peg.655.
TIGR	HI0685.
Phylogenomic databases
HOGENOM	P43799.
OMA	P43799. KTFLESC.
Enzyme and pathway databases
BioCyc	HINF71421:HI_0685-MON.
BRENDA	1.1.99.5. 109.
Family and domain databases
InterPro	IPR017752. Anaerobic_glycerol3P_DH_asu. IPR007419. BFD_Fer2_bd. IPR000447. FAD-dep_Gly3P_DH. IPR006076. FAD-dep_OxRdtase. [Graphical view]
Pfam	PF01266. DAO. 1 hit. PF04324. Fer2_BFD. 1 hit. [Graphical view]
PRINTS	PR01001. FADG3PDH.
TIGRFAMs	TIGR03377. glycerol3P_GlpA. 1 hit.
PROSITE	PS00977. FAD_G3PDH_1. 1 hit. PS00978. FAD_G3PDH_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GLPA_HAEIN

Accession

Primary (citable) accession number: P43799

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	June 16, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)