O85675 (ANTDC_ACIAD) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Anthranilate 1,2-dioxygenase electron transfer component

Including the following 2 domains:

1. Ferredoxin
2. Ferredoxin--NAD(+) reductase
   EC=1.18.1.3

Gene names

Name:	antC
Ordered Locus Names:	ACIAD2671

Organism

Acinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP]

Taxonomic identifier

62977 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

Protein attributes

Sequence length	343 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Electron transfer component of anthranilate 1,2-dioxygenase system. Ref.3
Catalytic activity	Reduced ferredoxin + NAD+ = oxidized ferredoxin + NADH. Ref.3
Cofactor	FAD. Ref.3 Binds 1 2Fe-2S cluster per subunit. Ref.3
Pathway	Aromatic compound metabolism; anthranilate degradation via hydroxylation; catechol from anthranilate: step 1/1. Ref.3
Subunit structure	Monomer. It is part of the anthranilate dioxygenase two component enzyme system. The other component is an oxygenase component consisting of 3 large (AntA) and 3 small (AntB) subunits. Ref.3
Sequence similarities	Belongs to the bacterial ring-hydroxylating dioxygenase ferredoxin reductase family. Contains 1 2Fe-2S ferredoxin-type domain. Contains 1 FAD-binding FR-type domain.

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Ligand	2Fe-2S FAD Flavoprotein Iron Iron-sulfur Metal-binding NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	aromatic compound catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: InterPro ferredoxin-NAD+ reductase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 343	343	Anthranilate 1,2-dioxygenase electron transfer component		PRO_0000415159
Regions
	Domain	3 – 96	94	2Fe-2S ferredoxin-type
	Domain	103 – 206	104	FAD-binding FR-type
	Region	98 – 338	241	Ferredoxin-reductase
Sites
	Metal binding	40	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	45	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	48	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	80	1	Iron-sulfur (2Fe-2S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	O85675 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: A8CEE4658B41234A	FASTA	343	38,549
	10 20 30 40 50 60 MNHSVALNFA DGKTFFIAVQ EDELLLDAAV RQGINLPLDC REGVCGTCQG TCETGIYEQE 70 80 90 100 110 120 YVDEDALSER DLAKRKMLAC QTRVKSNAAF YFDHHSSICN AGETLKIATV VTGVELVSET 130 140 150 160 170 180 TAILHLDASQ HVKQLDFLPG QYARLQIPDT DDWRSYSFAN RPNASNQLQF LIRLLPNGVM 190 200 210 220 230 240 SNYLRERCQV GQTLIMEAPL GSFYLREVER PLVFIAGGTG LSAFLGMLDN IAEQPNQPSV 250 260 270 280 290 300 HLYYGVNTEA DLCEQKRLTT YAERIKNFSY HPIISKASEQ WQGKSGFIHE HLDKNQLSEQ 310 320 330 340 SFDMYLCGPP PMIEAVKTWL DEQAIADCHI YSEKFLQSNT AKT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Similarities between the antABC-encoded anthranilate dioxygenase and the benABC-encoded benzoate dioxygenase of Acinetobacter sp. strain ADP1." Bundy B.M., Campbell A.L., Neidle E.L. J. Bacteriol. 180:4466-4474(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ADP1.
[2]	"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium." Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C. Nucleic Acids Res. 32:5766-5779(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ADP1.
[3]	"Characterization and evolution of anthranilate 1,2-dioxygenase from Acinetobacter sp. strain ADP1." Eby D.M., Beharry Z.M., Coulter E.D., Kurtz D.M. Jr., Neidle E.L. J. Bacteriol. 183:109-118(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, SUBUNIT. Strain: ADP1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF071556 Genomic DNA. Translation: AAC34815.1. CR543861 Genomic DNA. Translation: CAG69426.1.
RefSeq	YP_047248.1. NC_005966.1.
3D structure databases
HSSP	HSSP built from PDB template 1KRH based on UniProtKB P07771.
ProteinModelPortal	O85675.
ModBase	Search...
Protein-protein interaction databases
STRING	62977.ACIAD2671.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAG69426; CAG69426; ACIAD2671.
GeneID	2880359.
KEGG	aci:ACIAD2671.
PATRIC	20742941. VBIAciSp98416_2411.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0543.
HOGENOM	HOG000263663.
KO	K11311.
OMA	ASTLCHA.
ProtClustDB	PRK11872.
Enzyme and pathway databases
BioCyc	ASP62977:GJVV-2485-MONOMER. MetaCyc:MONOMER-7504.
UniPathway	UPA01016; UER01026.
Family and domain databases
Gene3D	3.10.20.30. 1 hit.
InterPro	IPR001041. 2Fe-2S_ferredoxin-type. IPR006058. 2Fe2S_fd_BS. IPR012675. Beta-grasp_dom. IPR017927. Fd_Rdtase_FAD-bd. IPR008333. OxRdtase_FAD-bd_dom. IPR001433. OxRdtase_FAD/NAD-bd. IPR001221. Phe_hydroxylase. IPR017938. Riboflavin_synthase-like_b-brl. [Graphical view]
Pfam	PF00970. FAD_binding_6. 1 hit. PF00111. Fer2. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view]
PRINTS	PR00410. PHEHYDRXLASE.
SUPFAM	SSF54292. Ferredoxin. 1 hit. SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
PROSITE	PS00197. 2FE2S_FER_1. 1 hit. PS51085. 2FE2S_FER_2. 1 hit. PS51384. FAD_FR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ANTDC_ACIAD

Accession

Primary (citable) accession number: O85675

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 25, 2012
Last sequence update:	November 1, 1998
Last modified:	May 1, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program