Reviewed, UniProtKB/Swiss-Prot P33110 (ARLY_ANSAN)

Names and origin

Protein names

Recommended name:
    Argininosuccinate lyase
      Short name=ASAL
    EC=4.3.2.1
Alternative name(s):
    Arginosuccinase
    Delta crystallin

Gene names

Name:

ASL

Organism

Anser anser anser (Western graylag goose)

Taxonomic identifier

8844 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Anseriformes › Anatidae › Anser

Protein attributes

Sequence length	466 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Delta crystallin, the principal crystallin in embryonic lens, is found only in birds and reptiles. This protein also functions as an enzymatically active argininosuccinate lyase.
Catalytic activity	2-(N(omega)-L-arginino)succinate = fumarate + L-arginine. Ref.2
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.
Subunit structure	Homotetramer.
Tissue specificity	Eye lens. Ref.1
Sequence similarities	Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
Biophysicochemical properties	Kinetic parameters: Vmax=19 nmol/min/mg enzyme

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis
Cellular component	Eye lens protein
Molecular function	Lyase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	arginine biosynthetic process via ornithine Inferred from electronic annotation. Source: InterPro
Molecular function	argininosuccinate lyase activity Ref.2 Inferred from direct assay. Source: UniProtKB structural constituent of eye lens Ref.2 Traceable author statement. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 466

466

Argininosuccinate lyase

PRO_0000137718

Regions

Region

112 – 114

3

Substrate binding By similarity

Sites

Active site

160

1

Proton acceptor; shared with tetrameric partner 2 By similarity

Active site

281

1

Proton acceptor; shared with tetrameric partner 1 By similarity

Active site

294

1

Charge relay system; shared with tetrameric partner 1 By similarity

Binding site

27

1

Substrate By similarity

Binding site

89

1

Substrate By similarity

Binding site

159

1

Substrate; shared with tetrameric partner 2 By similarity

Binding site

287

1

Substrate; shared with tetrameric partner 1 By similarity

Binding site

321

1

Substrate By similarity

Binding site

326

1

Substrate By similarity

Binding site

329

1

Substrate By similarity

Secondary structure

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466

Helix Strand Turn

Details...

Helix

21 – 23

3

Helix

28 – 31

4

Helix

32 – 34

3

Helix

35 – 51

17

Helix

57 – 75

19

Helix

88 – 100

13

Helix

103 – 108

6

Helix

113 – 149

37

Turn

150 – 152

3

Beta strand

154 – 159

6

Beta strand

162 – 168

7

Helix

169 – 194

26

Beta strand

195 – 197

3

Turn

202 – 205

4

Helix

213 – 219

7

Beta strand

223 – 225

3

Helix

229 – 234

6

Helix

237 – 263

27

Turn

266 – 268

3

Beta strand

270 – 272

3

Helix

275 – 277

3

Helix

291 – 314

24

Helix

323 – 327

5

Helix

328 – 352

25

Helix

357 – 362

6

Helix

366 – 369

4

Helix

370 – 378

9

Turn

379 – 381

3

Helix

384 – 401

18

Helix

405 – 407

3

Helix

410 – 416

7

Helix

424 – 427

4

Helix

430 – 435

6

Beta strand

442 – 444

3

Helix

445 – 461

17

Sequences

	Sequence		Length	Mass (Da)
	P33110-1 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: 2D346902B8821C10	FASTA	466	51,372
	10 20 30 40 50 60 MASEGDKLMG GRFVGSTDPI MQMLSTSMST EQRLSEVDIQ ASIAYAKALE KAGILTKTEL 70 80 90 100 110 120 EKILSGLEKI SEEWSKGVFV VTQSDEDIHT ANERRLKELI GDIAGKLNTG RSRNEQVVTD 130 140 150 160 170 180 LKLFMKNSLS VISTHLLQLI KTLVERAAIE IDVILPGYTH LQKAQPIRWS QFLLSHAVAL 190 200 210 220 230 240 TRDSERLGEV KRRINVLPLG SGALAGNPLD IDREMLRSEL DFASISLNSM DAISERDFVV 250 260 270 280 290 300 EFLSVATLLM IHLSKMAEDL IIYSTSEFGF LTLSDAFSTG SSLMPQKKNP DSLELIRSKA 310 320 330 340 350 360 GRVFGRLASI LMVLKGLPST YNKDLQEDKE AVFDVVDTLT AVLQVATGVI STLQISKENM 370 380 390 400 410 420 EKALTPEMLS TDLALYLVRK GMPFRQAHTA SGKAVHLAET KGITINNLTL EDLKSISPLF 430 440 450 460 SSDVSQVFNF VNSVEQYTAM GGTAKSSVTT QIEHLRELMK KQKEQA

References

[1]	"Facile cloning and sequence analysis of goose delta-crystallin gene based on polymerase chain reaction." Yu C.W., Chiou S.-H. Biochem. Biophys. Res. Commun. 192:948-953(1993) [PubMed: 8484796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Tissue: Lens.
[2]	"The effect of N-terminal truncation on double-dimer assembly of goose delta-crystallin." Lee H.J., Lai Y.H., Wu S.Y., Chen Y.H. Biochem. J. 392:545-554(2005) [PubMed: 16101585] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-466, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X70855 mRNA. Translation: CAA50208.1.

PIR

JN0486.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1XWO	X-ray	2.80	A/B/C/D	2-466	[»]

ModBase

Search...

Phylogenomic databases

HOVERGEN

P33110.

Family and domain databases

InterPro

IPR009049. Argininosuccinate_lyase.
IPR003031. D_crystallin.
IPR000362. Fumarate_lyase.
IPR020557. Fumarate_lyase_CS.
IPR008948. L-Aspartase-like.
[Graphical view]

PANTHER

PTHR11444:SF3. argH. 1 hit.

Pfam

PF00206. Lyase_1. 1 hit.
[Graphical view]

PRINTS

PR00145. ARGSUCLYASE.
PR00149. FUMRATELYASE.

TIGRFAMs

TIGR00838. argH. 1 hit.

PROSITE

PS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ARLY_ANSAN

Accession

Primary (citable) accession number: P33110

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	February 9, 2010
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)