A5AB29 (A5AB29_ASPNC) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Catalytic activity: L-glutamate = 4-aminobutanoate + CO2 EMBL CAK96663.1
EC=4.1.1.15 EMBL CAK96663.1

Gene names

ORF Names:

An08g08840 EMBL CAK96663.1

Organism

Aspergillus niger (strain CBS 513.88 / FGSC A1513) [Complete proteome]

Taxonomic identifier

425011 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus › Aspergillus niger

Protein attributes

Sequence length	515 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Cofactor	Pyridoxal phosphate By similarity. RuleBase RU000382
Sequence similarities	Belongs to the group II decarboxylase family. RuleBase RU000382

Ontologies

Keywords
Ligand	Pyridoxal phosphate RuleBase RU000382
Molecular function	Lyase RuleBase RU000382 EMBL CAK96663.1
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	glutamate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	glutamate decarboxylase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	A5AB29 [UniParc]. Last modified June 12, 2007. Version 1. Checksum: 1F3F6D1D28095766	FASTA	515	58,498
	10 20 30 40 50 60 MVHLAQVKRD SDVEKTAQQV GSIQLDSAED DAFYSSVYGT RFATEQLPST EMPEREMPRE 70 80 90 100 110 120 VAYRMIKDEL SLDGNPMLNL ASFVTTYMEE EVEKLMTESF SKNFIDYEEY PQSAEIQNRC 130 140 150 160 170 180 VNMIARLFNA PTDSDDEHPM GTSTIGSSEA IMLGTLAMKR RWQNKRRAEG KDASKPNIVM 190 200 210 220 230 240 NSAVQVCWEK AARYFDVEER YVYCTEDRYV IDPKQAVDLV DENTIGICAI LGTTYTGEYE 250 260 270 280 290 300 DVKAINDLLV ERGIDCPIHV DAASGGFVAP FVAPNLEWDF RLSKVVSINV SGHKYGLVYP 310 320 330 340 350 360 GVGWVVWRSP EYLPKELIFN INYLGAEQAS FTLNFSKGAS QVIGQYYQMI RLGKRGYRSI 370 380 390 400 410 420 MTNITRTADY LADQLEQLGF VIMSERRGKG LPLVAFRLPA DRDSEQFDEF ALAHQLRERG 430 440 450 460 470 480 WIVPAYTMAP NSNSLKLMRV VVREDFSKNR CDALLADIKL ALKTLSDMDK AMLERYTHHV 490 500 510 RVHSTNSHKS KHVHPHYKNE SHSLQGKHGK THGVC

References

[1]

"Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88." Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M. , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H. Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CBS 513.88 / FGSC A1513.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM270178 Genomic DNA. Translation: CAK96663.1.
RefSeq	XP_001392995.1. XM_001392958.2.
3D structure databases
ProteinModelPortal	A5AB29.
ModBase	Search...
Protein-protein interaction databases
STRING	5061.CADANGAP00007073.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADANGAT00007207; CADANGAP00007073; CADANGAG00007207.
GeneID	4983202.
KEGG	ang:ANI_1_1216074.
Phylogenomic databases
HOGENOM	HOG000070228.
KO	K01580.
OrthoDB	EOG47Q1F8.
Family and domain databases
Gene3D	3.40.640.10. 1 hit.
InterPro	IPR010107. Glutamate_decarboxylase. IPR002129. PyrdxlP-dep_de-COase. IPR015424. PyrdxlP-dep_Trfase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
PANTHER	PTHR11999:SF1. PTHR11999:SF1. 1 hit.
Pfam	PF00282. Pyridoxal_deC. 1 hit. [Graphical view]
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMs	TIGR01788. Glu-decarb-GAD. 1 hit.
ProtoNet	Search...

Entry information

Entry name

A5AB29_ASPNC

Accession

Primary (citable) accession number: A5AB29

Entry history

Integrated into UniProtKB/TrEMBL:	June 12, 2007
Last sequence update:	June 12, 2007
Last modified:	April 3, 2013
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)